Autophagy [JOURNAL]
Sun
200 papers
Increased macrophage autophagy with unique polarization in rheumatoid synovium.
Huang H, Takakubo Y, Takeda Y … +7 more , Uno T, Satake H, Asao H, Futakuchi M, Yang YP, Goodman SB, Takagi M
Autophagy · 2026 Jun · PMID 41729612 · Full text
Rheumatoid arthritis (RA) is characterized by synovitis and joint destruction, with macrophages playing a crucial role in pathogenesis. Macroautophagy/autophagy is essential for cellular homeostasis and has been implicat...
Rheumatoid arthritis (RA) is characterized by synovitis and joint destruction, with macrophages playing a crucial role in pathogenesis. Macroautophagy/autophagy is essential for cellular homeostasis and has been implicated in RA, but its role in macrophage polarization remains unclear. This study aimed to investigate the expression of autophagy-related molecules and macrophage phenotypes in RA synovium. Synovial tissues from patients with RA were analyzed and compared with samples of osteoarthritis (OA) and less-inflammatory synovium (LIS) obtained at immediate surgery for hip fracture. Synovitis severity was histologically assessed, and cellular ultrastructure was examined via electron microscopy. Immunohistochemistry, western blot, and flow cytometry were used to analyze autophagy-related molecules and macrophage phenotypes. RA synovium exhibited significant inflammation, with macrophage-like synovial cells and intimal macrophages showing abundant autophagy-related structures in comparison to those of OA and LIS. Autophagy markers, BECN1 (beclin 1), WIPI2, ATG5, ATG16L1, LC3B, ATG3, SQSTM1, and LAMP1, were highly expressed in CD68 macrophages but less in CD248/TEM-1 fibroblasts. Western blot confirmed higher levels of autophagy-related proteins in RA synovial tissue compared with OA and LIS. Macrophage polarization analysis identified M1-like (NOS2/iNOS, CD86), M2-like (CD163, MRC1/CD206, MERTK), and M1/M2-like (CD86 MRC1 NOS2 CD163) populations. M1/M2-like macrophages showed the highest autophagy-related molecule expression. Autophagy is strongly associated with macrophage polarization in RA synovium. M1/M2-like macrophages, highly enriched in autophagy markers, may play an anti-inflammatory role in modulating inflammation and tissue repair. These findings suggest a potential autophagy-mediated regulatory mechanism in RA macrophage function.s: ATG: autophagy related; BECN1: beclin 1; IL: interleukin; LAMP1: lysosomal associated membrane protein 1; LIS: less-inflammatory synovium; MAP1LC3/LC3: microtubule sssociated protein 1 light chain 3; MFI: mean fluorescence intensity; OA: osteoarthritis; PG: phagophore; RA: rheumatoid arthritis. SQSTM1: sequestosome 1; TNF: tumor necrosis factor; WIPI2: WD repeat domain, phosphoinositide interacting 2.
A switchable role of neuronal BNIP3L/NIX in mitochondrial fate: fission or finish.
Mo X, Zhang X, Zhang X
Autophagy · 2026 May · PMID 41712231 · Full text
BNIP3L/NIX is a mitophagy receptor highly expressed in the brain. Unlike most mitophagy receptors that are recruited to mitochondria only upon stress, BNIP3L constitutively localizes to the mitochondrial outer membrane,...
BNIP3L/NIX is a mitophagy receptor highly expressed in the brain. Unlike most mitophagy receptors that are recruited to mitochondria only upon stress, BNIP3L constitutively localizes to the mitochondrial outer membrane, suggesting functions beyond stress-induced mitophagy. Here, we identify a non-mitophagic role of BNIP3L in neuronal physiology. Conditional deletion of in glutamatergic neurons of the basolateral amygdala selectively impairs contextual fear memory in mice, a phenotype rescued by both wild-type BNIP3L and a mitophagy-deficient BNIP3L mutant lacking the LC3-interacting region motif. Mechanistically, BNIP3L competitively binds AMP-activated protein kinase (AMPK), thereby relieving AMPK-dependent inhibitory phosphorylation of DNM1L/DRP1 (dynamin 1 like) at Ser637. This interaction promotes rapid mitochondrial fission, supporting synaptic energy availability during memory encoding. Together, these findings reveal a switchable function of BNIP3L in neurons, acting either to acutely regulate mitochondrial dynamics to meet energetic demand or to engage mitophagy when mitochondrial function becomes compromised.
Alphaherpesvirus UL48 homologs degrade STING1 by selective autophagy.
Kong Z, Sun X, Zhai X … +11 more , Fan S, Liu R, Hu W, Guan K, Zhang Y, He W, Zhang Y, Wan B, Li N, Kong Z, Zhang G
Autophagy · 2026 Apr · PMID 41697162 · Full text
Alpha-herpesviruses have evolved strategies to break through immune defenses and cause severe host damage. Here, we demonstrate that the tegument protein UL48 in pseudorabies virus (PRV) inhibits type I interferon signal...
Alpha-herpesviruses have evolved strategies to break through immune defenses and cause severe host damage. Here, we demonstrate that the tegument protein UL48 in pseudorabies virus (PRV) inhibits type I interferon signaling by triggering STING1 degradation via a selective macroautophagy/autophagy pathway. Mechanistically, UL48 recruits the E3 ligase TRIM21 (tripartite motif containing 21), which catalyzes the ubiquitination of STING1 to form a K33/K63 linkage and is captured by the cargo receptor CALCOCO2/NDP52 for lysosomal degradation. In addition, multiple α-herpesvirus tegument protein UL48 homologs also target STING1 for degradation. Importantly, this phenotype was also observed in other herpesviruses driven by PRV UL48 homologs (herpes simplex virus-1 [HSV-1] and cercopithecine alphaherpesvirus 2 [CHV-2]). In addition, UL48-deficient PRV and HSV-1 mutant viruses attenuated pathogenicity in mice. In conclusion, this study describes a novel mechanism by which α-herpesviruses utilize UL48 proteins to promote viral escape from the host immune response.: 3-MA: 3-methyladenine; B-DNA: poly (dA:dT); BNIP3L/Nix: BCL2 interacting protein 3 like; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; cGAMP: cyclic GMP-AMPP; CGAS: cyclic GMP-AMP synthase; CHX: cyclohexane; CHV-2: cercopithecine herpesvirus 2; CQ: chloroquine; DAPI: 4',6-diamidino-2-phenylindole; DMSO: dimethyl sulfoxide; ER: endoplasmic reticulum; GFP: green fluorescent protein; H&E: hematoxylin and eosin; HSV-1: herpes simplex virus 1; IRF3: interferon regulatory factor 3; LIR: LC3-interacting region; MAP1LC3A/LC3: microtubule associated protein 1 light chain 3 alpha; MG132: cbz-leu-leu-leucinal; NBR1: NBR1 autophagy cargo receptor; OPTN: optineurin; PRV: pseudorabies virus; sgRNA: single guide RNA; siRNA: small interfering RNA; SQSTM1/p62: sequestosome 1; STING1/STING: stimulator of interferon response cGAMP interactor 1; TBK1: TANK binding kinase 1; TOLLIP: toll interacting protein.
Ferritinophagy and organ injury.
Shao N, Yu H, Li X … +6 more , Han M, Chen C, Zhu J, Tang Y, Dong J, Chen H
Autophagy · 2026 Jun · PMID 41692973 · Full text
Ferritinophagy is a selective form of macroautophagy/autophagy that mediates the degradation of ferritin complexes, releasing stored iron, and maintaining intracellular iron homeostasis. Proper regulation of ferritinopha...
Ferritinophagy is a selective form of macroautophagy/autophagy that mediates the degradation of ferritin complexes, releasing stored iron, and maintaining intracellular iron homeostasis. Proper regulation of ferritinophagy is essential for cellular adaptation to metabolic stress, whereas dysregulation disrupts iron balance and contributes to pathological processes. Excessive ferritinophagy leads to iron overload and reactive oxygen species accumulation, driving oxidative stress, ferroptosis, and inflammation, which are key contributors to cellular injury and progressive organ dysfunction. Despite advances in our understanding of autophagy and ferroptosis, the specific role of ferritinophagy in organ-specific injury remains unclear. In this review, we provide a comprehensive overview of the molecular mechanisms of ferritinophagy and critically examine its emerging roles in the pathogenesis of injuries to the heart, liver, lungs, and kidneys. We further highlight the therapeutic potential of targeting ferritinophagy and propose future research directions aimed at harnessing this pathway for the treatment of organ injuries. 3-MA: 3-methyladenine; ACO1/IRP1: aconitase 1; AKI: acute kidney injury; ARDS: acute respiratory distress syndrome; ATG: autophagy related; BECN1: beclin 1; CARM1/PRMT4: coactivator associated arginine methyltransferase 1; CIRBP: cold inducible RNA binding protein; CKD: chronic kidney disease; COPD: chronic obstructive pulmonary disease; ELAVL1: ELAV like RNA binding protein 1; Fer-1: ferrostatin-1; FTH1: ferritin heavy chain 1; GABARAP: GABA type A receptor-associated protein; GPX4: glutathione peroxidase 4; HAMP/hepcidin: hepcidin antimicrobial peptide; HCC: hepatocellular carcinoma; HERC2: HECT and RLD domain containing E3 ubiquitin protein ligase 2; HSCs: hepatic stellate cells; IL13: interleukin 13; IL6: interleukin 6; I/R: ischemia-reperfusion; IRE: iron-responsive element; IREB2/IRP2: iron responsive element binding protein 2; LPS: lipopolysaccharide; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MDA: malondialdehyde; MIOX: myo-inositol oxygenase; NCOA4: nuclear receptor coactivator 4; NFE2L2/Nrf2: NFE2 like bZIP transcription factor 2; ROS: reactive oxygen species; SIRT1: sirtuin 1; SLC40A1/ferroportin: solute carrier family 40 member 1; STAT3: signal transducer and activator of transcription 3; STEAP3: STEAP3 metalloreductase; TFRC/TfR1: transferrin receptor; USP11: ubiquitin specific peptidase 11; YAP1: Yes1 associated transcriptional regulator.
Phase separation of OPTN initiates mitophagy to orchestrate craniofacial bone mineralization.
Liu H, Lu Z, Zhang X … +8 more , Wang Y, Ge X, Chen S, Shi Y, Yan J, Xu R, Ma J, Guo S
Autophagy · 2026 May · PMID 41692957 · Full text
Recently, mitophagy-mediated bone mineralization of mesenchymal stem cells has emerged as another bone formation pattern, but whether mitophagy-mediated bone mineralization shapes craniofacial development remains unknown...
Recently, mitophagy-mediated bone mineralization of mesenchymal stem cells has emerged as another bone formation pattern, but whether mitophagy-mediated bone mineralization shapes craniofacial development remains unknown. Here, we demonstrate that loss of OPTN, a keystone macroautophagy/autophagy receptor, impairs mitophagy and acidic calcium phosphate (ACP) transport in orofacial bone mesenchymal stem cells (OMSCs), leading to craniofacial bone mineralization defects. We substantiate that OPTN undergoes LLPS both and , driven by S173 phosphorylation within its intrinsically disordered N-terminal domain (NTD), facilitating the association of OPTN complexes with phagophore membranes. Additionally, the ubiquitin-binding domain (UBD) in OPTN's C-terminal domain (CTD) also promotes LLPS to recruit ubiquitin-modified mitochondria. Physiochemically, mutations at the conserved sites in human OPTN (S173A and D474N) disrupt the OPTN LLPS, as validated in mouse and zebrafish, thereby inhibiting mitophagy and impairing bone mineralization. Together, our findings reveal a new mechanism through which OPTN LLPS couples mitophagy-mediated mineralization to craniofacial bone development, highlighting its potential as a therapeutic target for treating orofacial malformations via modulation of mitophagy.: 1, 6HD: 1, 6-hexanediol; ACP: acidic calcium phosphate; ALP: alkaline phosphatase; ARS: Alizarin Red staining; BFR/BS: bone formation rate per bone surface; Baf-A1: bafilomycin A; CCCP: carbonyl cyanide 3-chlorophenylhydrazone; CTD: C-terminal domain; dpf: days post-fertilization; EDS: energy dispersive spectroscopy; FL: full length; FRAP: fluorescence recovery after photobleaching; hpf: 24h post-fertilization; IDR: intrinsically disordered region; IHC: immunohistochemistry; LLPS: liquid-liquid phase separation; LC-MS/MS: liquid chromatography-tandem mass spectrometry; MAR: mineral apposition rate; MS/BS: mineralizing surface per bone surface; NTD: N-terminal domain; ODM: osteogenic differentiation medium; OMSCs: orofacial bone mesenchymal stem cells; OPTN: optineurin; P1: postnatal day 1; P21: postnatal day 21; PDB: Paget disease of bone; PTMs: post-translational modifications; qRT-PCR: quantitative real-time PCR; S173: serine 173; STK4: serine/threonine kinase 4; SEM: scanning electron microscopy; TMD: tissue mineral density; TEM: transmission electron microscopy; UBD: ubiquitin-binding domain; Ub: ubiquitin.
Expression of IMD-CBM peptide induces the autophagic degradation of CAV1 (caveolin 1) to inhibit LDL transcytosis and retard diabetic atherosclerosis.
Wang L, Jia X, Bai X … +7 more , Zhao Y, Cheng W, Shu M, Shu Y, Zhang L, Wang R, Jin S
Autophagy · 2026 Jun · PMID 41686177 · Full text
Atherosclerosis is attributable to a series of diabetes-related complications. CAV1 (caveolin 1)-mediated low-density lipoprotein (LDL) particle transcytosis across endothelial cells (ECs) is the initial step of atherosc...
Atherosclerosis is attributable to a series of diabetes-related complications. CAV1 (caveolin 1)-mediated low-density lipoprotein (LDL) particle transcytosis across endothelial cells (ECs) is the initial step of atherosclerosis. MAP1LC3/LC3-interacting regions in the intramembrane domain (IMD) of CAV1 were buried in the caveolae and were not accessible for LC3B interaction, protecting CAV1 from autophagic degradation. However, the CSD domain of CAV1, exposed in the cytosol, directly interacted with a CBM domain of LC3B and inhibited autophagy. Therefore, the peptide IMD-CBM was constructed to induce the selective autophagic degradation of CAV1 and suppress LDL transcytosis in diabetic atherosclerosis. EC-specific expression of IMD-CBM was achieved using adenovirus. IMD-CBM directly interacted with CAV1 and LC3B in ECs, leading to the selective autophagic degradation of CAV1, activation of autophagy, and subsequent inhibition of LDL transcytosis. IMD-CBM promoted the autophagic degradation of CAV1 and consequently reduced the area of atherosclerotic plaques in diabetic atherosclerotic mice. Overall, IMD-CBM expedited the autophagic degradation of CAV1 and inhibited high glucose-induced LDL transcytosis, highlighting its potential as a novel translatable strategy for the management of diabetic atherosclerosis.: ACTB: actin beta; AKT/protein kinase B: AKT serine/threonine kinase; AMPK: 5'-adenosine monophosphate-activated protein kinase; CAV1: caveolin 1; CBM: CAV1-binding motif; CRP: C-reactive protein; CSD: CAV1-scaffolding domain; GFP: green fluorescent protein; HUVEC: human umbilical vein endothelial cell; EC: endothelial cell; FITC: fluorescein isothiocyanate; IL6: interleukin 6; IL10: interleukin 10; IMD: intramembrane domain; LDL: low-density lipoprotein; LIR: LC3-interacting region; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MTOR: mechanistic target of rapamycin kinase; NFKB/NF-κB: nuclear factor kappa B; NFKBIA/IκBα: NFKB inhibitor alpha; NO: nitric oxide; PBS: phosphate-buffered saline; PCR: polymerase chain reaction; PIK3C3/VPS34: phosphatidylinositol-3-kinase catalytic subunit type 3; Rapa: rapamycin; SAA: serum amyloid A; SQSTM1/p62: sequestosome 1; STZ: streptozotocin; TEM: transmission electron microscopy; TNF/TNF-α: tumor necrosis factor.
Mammalian lipophagy: process and function.
Zhao R, Dai E, Kang R … +6 more , Liu J, Klionsky DJ, Tang D, Qu Y, Lin Y, Zhang X
Autophagy · 2026 Jun · PMID 41681129 · Full text
Lipophagy, the selective autophagic degradation of lipid droplets (LDs), is a key mechanism for lipid homeostasis and cellular adaptation to metabolic and stress conditions. In mammals, lipophagy is governed by signaling...
Lipophagy, the selective autophagic degradation of lipid droplets (LDs), is a key mechanism for lipid homeostasis and cellular adaptation to metabolic and stress conditions. In mammals, lipophagy is governed by signaling pathways, LD-associated receptors (e.g. SQSTM1/p62, NBR1, OPTN, SPART, OSBPL8, DDHD2, VPS4A, ATG14, and TP53INP2), and transcription factors (TFEB, TFE3, FOXO1, PPARA, PPARG, and SREBF1/SREBP1) that coordinate LD recognition, sequestration, and lysosomal degradation. Dysregulated lipophagy contributes to the pathogenesis of metabolic and age-related diseases, including metabolic dysfunction-associated steatotic liver disease/nonalcoholic fatty liver disease (MASLD/NAFLD), alcoholic liver disease, diabetes, atherosclerosis, neurodegeneration and cancer. Several recent reviews have discussed lipophagy from different angles, including its roles in metabolic disorders, central nervous system diseases, and fundamental mechanisms across species. In contrast, this review focuses specifically on mammalian lipophagy by synthesizing the latest mechanistic insights into receptor-mediated recognition, transcriptional regulation, and signaling integration. We also outline unresolved questions and conceptual gaps - such as how lipophagy is selectively activated, how it coordinates with lipolysis, and whether distinct receptor codes exist in tissue- and disease-specific contexts - that remain unanswered in the current literature.: AMPK, AMP-activated protein kinase; ATG, autophagy related; ATG8s: mammalian Atg8-family proteins; C1P: ceramide-1-phosphate; CMA, chaperone-mediated autophagy; COPI, coatomer protein complex I; DENV, dengue virus; ER, endoplasmic reticulum; ESCRT: endosomal sorting complex required for transport; FFA: free fatty acid; HOPS, homotypic fusion and vacuole protein sorting; LDs, lipid droplets; LIR: LC3-interacting region; MASLD, metabolic dysfunction-associated steatotic liver disease; MTORC1: mechanistic target of rapamycin kinase complex 1; PE: phosphatidylethanolamine; PEDV: porcine epidemic diarrhea virus; PENV, porcine epidemic diarrhea virus; PtdIns3K-C1: class III phosphatidylinositol 3-kinase complex 1; PtdIns3P, phosphatidylinositol-3-phosphate; ROS, reactive oxygen species; SNARE: soluble NSF attachment protein receptor; SPG54: spastic paraplegia type 54; TAG: triacylglycerol/triglyceride; UBDs, ubiquitin-binding domains.
Mitophagy bridges glucose metabolism, inflammation and neuroprotection in astrocytes.
Hakansson H, Howden JH, Kittler JT
Autophagy · 2026 May · PMID 41677100 · Full text
Mitochondria regulate ATP production, calcium buffering, and apoptotic signaling, and clearing dysfunctional mitochondria by mitophagy is essential for cellular homeostasis. While PINK1-dependent mitophagy is well-charac...
Mitochondria regulate ATP production, calcium buffering, and apoptotic signaling, and clearing dysfunctional mitochondria by mitophagy is essential for cellular homeostasis. While PINK1-dependent mitophagy is well-characterized in neurons, its function in glial cells such as astrocytes is less understood. Our study demonstrates that PINK1-mitophagy in astrocytes occurs faster and with less spatial restriction compared to neurons. This pathway was specifically regulated in astrocytes by the glycolytic enzyme, HK2 (hexokinase 2), which forms a glucose-dependent complex with PINK1 following mitochondrial damage. Inflammation also induces HK2-PINK1 mitophagy, and its activation in astrocytes protects against cytokine-induced neuronal death. Our findings characterize a novel HK2-PINK1 pathway in astrocytes that bridges mitophagy, metabolism, and immune signaling.: HK2: hexokinase 2; PD: Parkinson disease; PINK1: PTEN induced kinase 1; S65: serine 65.
AMPK promotes TFEB transcriptional activity through dephosphorylation at both MTORC1-dependent and -independent sites.
Negoita F, Fraguas Bringas C, Hellberg K … +9 more , Luda KM, Liu H, Li Z, Cuenco J, Zhao JF, Sathe G, Ganley IG, Sapkota GP, Sakamoto K
Autophagy · 2026 Jun · PMID 41661247 · Full text
TFEB (transcription factor EB) is a critical regulator of lysosomal biogenesis, macroautophagy/autophagy and energy homeostasis through controlling expression of genes belonging to the coordinated lysosomal expression an...
TFEB (transcription factor EB) is a critical regulator of lysosomal biogenesis, macroautophagy/autophagy and energy homeostasis through controlling expression of genes belonging to the coordinated lysosomal expression and regulation network. AMP-activated protein kinase (AMPK) has been reported to phosphorylate TFEB at three conserved C-terminal serine residues (S466, S467, S469) and these phosphorylation events were reported to be essential for transcriptional activation of TFEB. In sharp contrast to this proposition, we demonstrate that AMPK activation leads to the dephosphorylation of the C-terminal sites. We show that a synthetic peptide encompassing the C-terminal serine residues of TFEB is a poor substrate of AMPK in vitro. Treatment of cells with an AMPK activator (MK-8722), glucose deprivation or MTOR inhibitor (torin1) robustly dephosphorylated TFEB not only at the MTORC1-targeted N-terminal serine sites, but also at the C-terminal sites. Loss of function of AMPK abrogated MK-8722- but not torin1-induced dephosphorylation and induction of the TFEB target genes. AMPK: 5'-adenosine monophosphate-activated protein kinase; ACAC/ACC: acetyl-CoA carboxylase; AICAR: 5-aminoimidazole-4-carbox-amide ribonucleotide; CLEAR: coordinated lysosomal expression and regulation; DKO: double knockout; DMEM: Dulbecco's modified Eagle's medium; DMSO: dimethyl sulfoxide; DQ-BSA: self-quenched BODIPY® dye conjugates of bovine serum albumin; KI: knock-in; KO: knockout; MEFs: mouse embryonic fibroblasts; MTORC1: mechanistic target of rapamycin kinase complex 1; RRAGC: Ras related GTP binding C; RPTOR: regulatory associated protein of MTOR complex 1; RPS6KA/RSK: ribosomal protein S6 kinase A; RPS6KB1/S6K1: ribosomal protein S6 kinase B1; RT-qPCR: reverse transcription quantitative polymerase chain reaction; TFE3: transcription factor binding to IGHM enhancer 3; TFEB: transcription factor EB; ULK1: unc-51 like autophagy activating kinase 1; WT: wild-type.
Regorafenib enhances anti-PDCD1/PD-1 therapeutic efficacy in colorectal cancer by promoting SQSTM1/p62-mediated CD274/PD-L1 degradation.
Zhu M, He Y, Lei S … +7 more , Lai X, Chen C, Ye K, Li D, Zhang H, Lai M, Jiang W
Autophagy · 2026 Jun · PMID 41655134 · Full text
Despite the clinical success of PDCD1/PD-1 and CD274/PD-L1 immune checkpoint blockade in multiple cancers, its efficacy in colorectal cancer (CRC) remains limited. Here, we report that the combination of the tyrosine kin...
Despite the clinical success of PDCD1/PD-1 and CD274/PD-L1 immune checkpoint blockade in multiple cancers, its efficacy in colorectal cancer (CRC) remains limited. Here, we report that the combination of the tyrosine kinase inhibitor regorafenib with PDCD1 blockade enhances anti-tumor immunity in CRC, both in clinical observations and preclinical models. Mechanistically, regorafenib acts as a molecular glue, directly promoting the interaction between CD274 and the selective autophagy receptor SQSTM1/p62, leading to SQSTM1-mediated autophagic degradation of CD274 and restoration of T cell-mediated cytotoxicity. In summary, these findings identify a previously unrecognized role of regorafenib in modulating tumor immune evasion and provide a mechanistic rationale for its combination with PDCD1 inhibitors in CRC treatment.: 3-MA: 3-methyladenine; ATG5: autophagy related 5; ATG7: autophagy related 7; CD274/PD-L1: CD274 molecule; CHX: cycloheximide; co-IP: co-immunoprecipitation; CQ: chloroquine; CRC: colorectal cancer; CTLs: cytotoxic T cells; ECD: extracellular domain; GZMB: granzyme B; ICD: intracellular domain; IF: immunofluorescence; IFNG/IFN-γ: interferon gamma; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; mCRC: metastatic colorectal cancer; mIF: multiplex immunofluorescence; MSS: microsatellite stable; ORRs: objective response rates; PDCD1/PD-1: programmed cell death 1; PDCD1i: PDCD1 inhibitor; pMMR: mismatch repair-proficient; PROTACs: proteolysis-targeting chimeras; SPR: surface plasmon resonance; SQSTM1/p62: sequestosome 1; TKI: multikinase inhibitor; TME: tumor microenvironment; WB: western blot; WT: wild-type.
Redirecting NEU (neuraminidase) antigen to autophagosomes confers enhanced cross-reactive T-cell immunity against heterosubtypic influenza virus infection.
Han Z, Pan W, Lai W … +10 more , Cui M, Li R, Deng L, Gao Y, Shi SJ, Gan J, Lahn BT, Chen YQ, Shu Y, Sun C
Autophagy · 2026 Jun · PMID 41655133 · Full text
NEU (neuraminidase) is a potential cross-reactive antigen for developing broadly protective influenza vaccine, but has suboptimal immunogenicity. We here report that, when NEU antigen was redirected into phagophores, and...
NEU (neuraminidase) is a potential cross-reactive antigen for developing broadly protective influenza vaccine, but has suboptimal immunogenicity. We here report that, when NEU antigen was redirected into phagophores, and subsequently autophagosomes, by fusing with MAP1LC3B/LC3B (microtubule associated protein 1 light chain 3 beta; NEU-LC3B), it could efficiently activate the autophagosome-lysosome-major histocompatibility complex class II (MHC II) compartment pathway, and thus substantially improve the magnitude, breadth, and polyfunctionality of NEU-specific T cell immunity in mice. Remarkably, we identified several novel NEU-specific T-cell epitopes in response to NEU-LC3B-based immunization. Furthermore, mice immunized with NEU-based constructs were challenged with homologous A/CA/04/09 (H1N1), heterologous within-subtype strain A/Puerto Rico/8/1934 (PR8) (H1N1), and heterosubtypic A/Aichi/2/1968 (H3N2) virus, and the results demonstrated that NEU-LC3B-based vaccine provided a sterilizing immunity to homologous strains and cross-protection against antigenically distinct heterosubtypic challenge. In addition, cell depletion experiment demonstrated that T-cell-mediated immunity contributed to the NEU-LC3B-mediated immune protection. Collectively, this engineered NEU antigen with optimal immunogenicity represents a promising strategy for developing broadly protective influenza vaccines.: BSA, bovine serum albumin; CQ, chloroquine; ELISpot, enzyme-linked immunosorbent spot; HA, hemagglutinin; ICS, intracellular cytokine staining; IFNG/IFN-γ, interferon gamma; LD50, Median Lethal Doses; MAP1LC3B/LC3B, microtubule associated protein 1 light chain 3 beta; NEU, neuraminidase; NP, nucleoprotein; PBS, phosphate-buffered saline; RAPA, rapamycin; SFC, spot-forming cells; SV, split vaccine; TCID, median tissue culture infectious dose; VSV, vesicular stomatitis virus; VSVΔG, VSV vector with the deletion of the gene.
Golgi fragmentation driven by the USP11-ITCH axis triggers autolysosomal failure in neurodegeneration.
Xiang Q, Liu Y, Wang J
Autophagy · 2026 May · PMID 41655130 · Full text
Golgi fragmentation is a prominent early hallmark of neurodegenerative diseases such as Alzheimer disease (AD) and amyotrophic lateral sclerosis (ALS), yet the shared molecular mechanisms underlying this phenomenon remai...
Golgi fragmentation is a prominent early hallmark of neurodegenerative diseases such as Alzheimer disease (AD) and amyotrophic lateral sclerosis (ALS), yet the shared molecular mechanisms underlying this phenomenon remain poorly understood. Here we identify the E3 ubiquitin ligase ITCH as a central regulator of Golgi integrity and proteostasis. Elevated ITCH disrupts both cis- and trans-Golgi networks, dislocates lysosomal hydrolase sorting factors, and impairs maturation of hydrolases. The ensuing lysosomal dysfunction leads to autophagosome accumulation and defective clearance of accumulated cytoplasmic toxic proteins like TARDBP/TDP-43. Genetic and pharmacological inhibition of ITCH restores autolysosomal degradation and protects neurons in both mammalian and models. Aberrant buildup of the deubiquitinase USP11 drives ITCH accumulation, intensifying neuronal proteotoxic stress in individuals with AD and ALS. These findings reveal a mechanistic pathway connecting Golgi disorganization, autolysosomal impairment, and proteotoxic stress in neurodegeneration.
SIRT3-mediated mitophagy by deacetylating ATP5F1A involved in the protective effects of SIGMAR1/Sigma-1 receptor against ferroptosis and microvascular hyperpermeability in lipopolysaccharide-induced acute lung injury.
Gao F, Li Z, Peng T … +9 more , Lin B, Wang X, Dai X, Ai C, Li G, Yang F, Lin X, Zhang Y, Li T
Autophagy · 2026 Jun · PMID 41655128 · Full text
Previous studies have shown that SIGMAR1/Sigma-1 receptor (sigma non-opioid intracellular receptor 1) provides protective effects against lipopolysaccharide (LPS)-induced acute lung injury (ALI), however the underlying m...
Previous studies have shown that SIGMAR1/Sigma-1 receptor (sigma non-opioid intracellular receptor 1) provides protective effects against lipopolysaccharide (LPS)-induced acute lung injury (ALI), however the underlying mechanism remains unclear. A recent study highlighted SIGMAR1's protective role against ferroptosis but did not fully elucidate the mechanism involved. Endothelial ferroptosis, which significantly affects microvascular permeability, has garnered increasing attention in research. In this context, we aimed to investigate how SIGMAR1 mitigates endothelial ferroptosis in ALI induced by LPS. PRE-084 (SIGMAR1 activator) inhibited endothelial ferroptosis and microvascular hyperpermeability in ALI induced by LPS; however, this effect was blocked by mitophagy inhibition. Knockout of worsened microvascular hyperpermeability and endothelial ferroptosis, but these effects were mitigated by activating SIRT3 (sirtuin 3). Conversely, inhibiting SIRT3 blocked the upregulation of SIGMAR1-mediated mitophagy and limited endothelial ferroptosis in ALI induced by LPS. In addition, LPS exposure led to the acetylation of lysine 498 in ATP5F1A/ATP5A1 (ATP synthase F1 subunit alpha). Importantly, downregulating ATP5F1A acetylation prevented the SIRT3 inhibition from blocking the effects of SIGMAR1 in facilitating mitophagy and preventing ferroptosis. Interestingly, downregulating ATP5F1A acetylation or activation of SIRT3 did not alter the effects of PRE-084 on ALI when mitophagy was inhibited, suggesting that SIGMAR1's ALI protective effects involve ATP5F1A- or SIRT3-dependent mitophagy. In conclusion, our findings indicate that SIGMAR1 alleviates endothelial ferroptosis and microvascular hyperpermeability in LPS-induced ALI through SIRT3-mediated mitophagy. Furthermore, the deacetylation of ATP5F1A at lysine 498 by SIRT3 is essential for SIGMAR1-mediated PRKN/parkin-dependent mitophagy.: ALI, acute lung injury; ARDS, acute respiratory distress syndrome; ATP, adenosine triphosphate; ATP5F1A, ATP synthase F1 subunit alpha; BCA, bicinchoninic acid; EB, Evans blue dye; ECM, endothelial cell medium; FBS, fetal bovine serum; FITC, fluorescein isothiocyanate; Fer-1, ferrostatin-1; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GFP-LC3, green fluorescent protein-microtubule associated protein 1 light chain 3 alpha; GPX4, glutathione peroxidase 4; GSH, glutathione; GSSG, glutathione disulfide; KO, knockout; LPS, lipopolysaccharide; LRRK2, leucine rich repeat kinase 2; MDA, malondialdehyde; MPMVECs, mouse pulmonary microvascular endothelial cells; MTT, 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide; PBS, phosphate-buffered saline; PECAM1/CD31, platelet and endothelial cell adhesion molecule 1; PRKN, parkin RBR E3 uniquitin protein ligase; ROS, reactive oxygen species; RSL3, RAS-selective lethal 3; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SIGMAR1, sigma non-opioid intracellular receptor 1; SIRT3, sirtuin 3; siRNA, small interfering RNA; TUNEL, terminal deoxyribonucleotidyl transferase-mediated deoxyuridine 5-triphosphate-digoxigenin nick end labeling; VHP, vascular hyperpermeability; W:D, wet:dry; WT, wild type.
Correction.
Autophagy · 2026 Feb · PMID 41640309 · Publisher ↗
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PRKN activation for mitophagy requires an NME3-regulated phosphatidic acid signal that separates mitochondria from endoplasmic reticulum tethering.
Chen CW, Chen YJ, Cuili X … +2 more , Chen YH, Chang ZF
Autophagy · 2026 May · PMID 41640016 · Full text
PINK1-dependent activation of PRKN/parkin on depolarized mitochondria causes mitophagy. The deficiency of NME3, a nucleoside diphosphate kinase/NDPK on the outer mitochondria membrane (OMM), is associated with a fatal ne...
PINK1-dependent activation of PRKN/parkin on depolarized mitochondria causes mitophagy. The deficiency of NME3, a nucleoside diphosphate kinase/NDPK on the outer mitochondria membrane (OMM), is associated with a fatal neurodegenerative disorder. Here, we report that NME3 deficiency impairs p-S65-ubiquitin (Ub)-dependent PRKN binding on depolarized mitochondria without involving the loss of Ub phosphorylation by PINK1. Our mechanistic investigation revealed that NME3 interacts with PLD6/MitoPLD to generate phosphatidic acid (PA) from cardiolipin on the OMM of damaged mitochondria after depolarization. This lipid signal is essential for positioning MFN2 nearby PINK1 for phosphorylation of Ub conjugates on MFN2, thus enabling the subsequent amplification of PRKN binding to mitochondria. We provide further evidence that mitochondria-endoplasmic reticulum (Mito-ER) tethering prohibits the proximity of MFN2 with PINK1 and PRKN amplification on mitochondria. Importantly, the loss of NME3-regulated PA signal causes Mito-ER tethering. Overall, our findings suggest that NME3 cooperates with PLD6 to generate PA as a critical step in Mito-ER untethering, allowing MFN2 access to PINK1 for p-S65-poly-Ub-dependent feedforward activation of PRKN. ACTB: actin beta; BDNF brain derived neurotrophic factor; CL: cardiolipin; CRISPR: clustered regularly interspaced short palindromic repeats; DAG: diacylglycerol; ER: endoplasmic reticulum; FCCP: carbonyl cyanide p-(trifluoromethoxy) phenylhydrazone; FRET: Förster resonance energy transfer; IF: immunofluorescence; KO: knockout; KD: knockdown; LPIN1: lipin 1; MERCS: mitochondria-endoplasmic reticulum contact sites; MFN2: mitofusin 2; Mito: mitochondria; OMM: outer mitochondrial membrane; p-Ub: phosphorylated ubiquitin; PA: phosphatidic acid; PD: Parkinson disease; PINK1: PTEN induced kinase 1; PLA: proximity ligation assay; PLD6/MitoPLD: phospholipase D family member 6; PRKN: parkin RBR E3 ubiquitin protein ligase; RA: retinoic acid; RT-qPCR: reverse transcription-quantitative polymerase chain reaction; TEM: transmission electron microscopy; TN-NME3: TOMM20-NΔ-NME3; TOMM20: translocase of outer mitochondrial membrane 20; TUBB: tubulin beta class I; Ub: ubiquitin; VDAC: voltage dependent anion channel; WB: western blot.
TGFB-inducible VASN (vasorin) promotes lysosomal acidification.
Yan J, Zhang Y, Choksi S … +4 more , Mikolaj MR, Harned A, Narayan K, Liu ZG
Autophagy · 2026 May · PMID 41630427 · Full text
The lysosome is not only a degradative organelle but also an essential platform for signal transduction, such as with MTOR signaling. The reciprocal regulation between the lysosome and MTOR is central to macroautophagy/a...
The lysosome is not only a degradative organelle but also an essential platform for signal transduction, such as with MTOR signaling. The reciprocal regulation between the lysosome and MTOR is central to macroautophagy/autophagy and metabolism. MTOR-mediated suppression of lysosomal acidification is important for lysosomal activity, autophagic flux, and cell survival. VASN is a transmembrane glycoprotein whose function is not fully understood. In the present study, we report that VASN is a TGFB-inducible protein and plays a crucial role in positively regulating lysosomal acidification. As a potential mechanism, we demonstrated that VASN localizes to the lysosome, interacts with lysosomal MTOR and STK11IP, and disrupts the binding of STK11IP to MTOR and the V-ATPase, which was recently reported to suppress lysosomal acidification. We found that VASN's function in modulating lysosomal activity is essential for optimal mitophagy induced by TGFB and terminal erythroid differentiation and is critical for the progression of mutant KRAS-driven lung cancer. Overall, our study identified VASN as a novel TGFB-inducible regulator of lysosomal function.: ATG5, autophagy related 5; BNIP3, BCL2 interacting protein 3; BNIP3L, BCL2 interacting protein 3 like; CLEM, correlative-light electron microscopy; DSP, dithiobis(succinimidyl propionate); EGFP, enhanced green fluorescent protein; EYFP, enhanced yellow fluorescent protein; FIB-SEM, focused ion beam-scanning electron microscopy; LAMP1, lysosomal-associated membrane protein 1; LysoIP, lysosomal immunoprecipitation; MAP1LC3B, microtubule-associated protein 1 light chain 3 beta; MTOR, mechanistic target of rapamycin kinase; RBCs, red blood cells; SMAD, SMAD family member; STK11IP, serine/threonine kinase 11 interacting protein; TEM, transmission electron microscopy; TGFB, transforming growth factor beta; TGOLN2/TGN38, trans-golgi network protein 2; TMEM192, transmembrane protein 192; V-ATPase, vacuolar-type H-translocating ATPase.
Mitochondrial transplantation ameliorates rheumatoid arthritis by targeting abnormal CGAS-STING1 signaling activation, autophagosome accumulation, and necroptosis.
Lee AR, Woo JS, Lee SY … +7 more , Shin Y, Jeon SB, Jo Y, Choi H, Park SH, Kang T, Cho ML
Autophagy · 2026 May · PMID 41623018 · Full text
Mitochondrial damage in fibroblast-like synoviocytes (FLSs) is a key factor involved in the development and progression of rheumatoid arthritis (RA). In this study, we investigated the role of mitochondrial dysfunction o...
Mitochondrial damage in fibroblast-like synoviocytes (FLSs) is a key factor involved in the development and progression of rheumatoid arthritis (RA). In this study, we investigated the role of mitochondrial dysfunction of FLSs in the pathogenesis of RA. We induced inflammation by stimulating FLSs with TNF and IL17. Then, we transplanted fresh mitochondria into stimulated FLSs and evaluated the mitochondrial and lysosomal functions, macroautophagic/autophagic activity, and the STING1-associated cell death pathway. Next, we transplanted mitochondria or gold nanoparticle-conjugated mitochondria (GNP-Mito) into collagen-induced arthritis (CIA) mice and evaluated their therapeutic effects . Mitochondrial and lysosomal activities were decreased and autophagosomes accumulated in the stimulated FLSs. Furthermore, the STING1 signaling pathway and STING1-associated cell death were increased in the inflammatory condition. Mitochondrial transplantation into stimulated FLSs enhanced the mitochondrial and lysosomal activities and activated the autophagic activity, as demonstrated by decreased numbers of autophagosomes and increased numbers of autolysosomes. Mitochondrial transplantation decreased and increased the T17 and T populations, respectively. Mitochondrial function and autophagic activity were enhanced by mitochondrial transplantation. Taken together, our results demonstrate that mitochondrial dysfunction in FLSs plays a pivotal role in the pathophysiology of RA and mitochondrial transplantation has therapeutic potential for RA development and progression.: ATP:adenosine triphosphate; CGAS: cyclic GMP-AMP synthase; CIA:collagen-induced arthritis; FLS: fibroblast-like synoviocytes; GNP:gold nanoparticle; ROS: reactive oxygen species; SQSTM1/p62:sequestosome 1; STING1: stimulator of interferon response cGAMPinteractor 1; MAP1LC3B/LC3B: microtubule associated protein 1 lightchain 3 beta.
Kitasamycin overcomes ferroptosis and immunotherapy resistance by targeting the HUWE1-NCOA4-FTH1 axis.
Li D, Dian Y, Li L … +16 more , Du S, Meng Y, Yao L, Zhou Q, Xiong Y, Sun Y, Su H, Li Y, Guo Z, Ge Y, Liu S, Zeng F, Chen X, Lu L, Su J, Deng G
Autophagy · 2026 May · PMID 41612599 · Full text
Clinicians typically avoid antibiotics use during immunotherapy due to concerns about reduced efficacy. However, cancer patients requiring antibiotics postoperatively or for infections urgently need options that provide...
Clinicians typically avoid antibiotics use during immunotherapy due to concerns about reduced efficacy. However, cancer patients requiring antibiotics postoperatively or for infections urgently need options that provide antimicrobial coverage while potentially enhancing, rather than impairing, immunotherapy. Restoring ferroptosis susceptibility represents a promising strategy to overcome immunotherapy resistance, yet the role of antibiotics in modulating ferroptosis and interacting with immunotherapy remains unexplored. In this study, we screened 96 FDA-approved antibiotics across seven pharmacological classes and identified the macrolide kitasamycin as a specific and potent ferroptosis sensitizer in vitro and in vivo. Mechanistically, kitasamycin competitively bound to HUWE1, inhibiting its E3 ubiquitin ligase activity, which stabilized NCOA4 and activated the NCOA4-FTH1 ferritinophagy axis. Single-cell transcriptomics, flow cytometry, and multiplex immunohistochemistry revealed that kitasamycin induced immunogenic ferroptosis and reshaped anti-tumor T-cell immunity. Critically, kitasamycin potentiated immune checkpoint blockade (ICB)-mediated ferroptosis and overcame ICB resistance across multiple preclinical melanoma models, including B16F10 subcutaneous tumors, BRAF-PTEN-driven spontaneous tumors, and human sourced peripheral blood mononuclear cells (HsPBMCs)-humanized mouse models. Clinically, a high NCOA4, low HUWE1 signature correlated with ferroptosis activation, increased T-cell infiltration, and improved survival in ICB-treated patients, suggesting its potential as a predictive biomarker. Our findings positioned kitasamycin as a promising adjunct to immunotherapy for cancer patients requiring concurrent antibiotic therapy.: FTH1: ferritin heavy chain 1; ICB: immune checkpoint blockade; IFNG: interferon gamma; mIHC: multiplex immunohistochemistry; scRNA-seq: single-cell RNA sequencing.
/Autophagy inactivation in mouse bone microenvironment promotes tumor development.
Trojani MC, Nollet M, Camuzard O … +9 more , Santucci-Darmanin S, Breuil V, Burel-Vandenbos F, Fradet L, Le Gall M, Salnot V, Heymann D, Carle GF, Pierrefite-Carle V
Autophagy · 2026 May · PMID 41612597 · Full text
Bone is an attractive site for cancer colonization, both for primary tumors such as osteosarcoma and for metastases of various malignancies. Preventing bone metastasis, which is associated with a poor prognosis, is a maj...
Bone is an attractive site for cancer colonization, both for primary tumors such as osteosarcoma and for metastases of various malignancies. Preventing bone metastasis, which is associated with a poor prognosis, is a major challenge and identifying the factors involved in skeletal tumoral development is crucial to improve survival. In the present work, we showed that inactivation of the macroautophagy/autophagy-essential gene in osteoblasts, the cells in charge of bone formation, stimulates osteosarcoma and breastbone metastasis growth as well as metastatic dissemination. We determined that inactivation leads to systemic inflammation and bone proteome modifications including translation downregulation, stress granule formation, and upregulation of fatty acid beta-oxidation. In addition, inactivation triggered lysosomal exocytosis through an autophagy-independent effect. Thus, our findings indicated that autophagy/ATG5 deficiency in the bone microenvironment generates a favorable environment for tumor development through several mechanisms and suggested that a bone-targeted autophagy inducer could be used to delay bone metastasis appearance. ACP5/TRAP : acid phosphatase 5, tartrate resistant; CHI3L1 : chitinase 3 like 1; COL1A1 : collagen type I alpha 1 chain; ECM: extracellular matrix ; FDR: false discovery rate; G3BP1 : G3BP stress granule assembly factor 1; GSEA : gene set enrichment analyses; IFNG : interferon gamma; IL1B : interleukin 1 beta; IL23A : interleukin 23; IPA: ingenuity pathway analyses; ITGAX/CD11c : integrin subunit alpha X; KO : knockout; LAMP1 : lysosomal associated membrane protein 1; LGALS3 : galectin 3; LLOMe : L-leucyl-L-leucine methyl ester; OB : osteoblast; OC : osteoclast; PDCD6IP/Alix : programmed cell death 6 interacting protein; PDK4 : pyruvate dehydrogenase kinase 4.
PRKAB2 as a tumor suppressor in renal cell carcinoma: inhibiting mitophagy via the LRPPRC-PRKN/parkin interaction and cardiolipin biosynthesis.
Chen K, Zhang Y, Ruan H … +10 more , Wei Z, Wang K, Cao Q, Wang Q, Dong Z, Wu Y, Yang H, Liu L, Liu Y, Zhang X
Autophagy · 2026 May · PMID 41612594 · Full text
Renal cell carcinoma (RCC) is characterized by dysregulated lipid metabolism and a high propensity for developing resistance to targeted therapies. Mitophagy is a key process involved in the progression of various cancer...
Renal cell carcinoma (RCC) is characterized by dysregulated lipid metabolism and a high propensity for developing resistance to targeted therapies. Mitophagy is a key process involved in the progression of various cancers, including RCC. Here, using genome-wide CRISPR screening, we identified PRKAB2 as a crucial tumor suppressor in RCC. Reduced PRKAB2 expression correlated with poor prognosis and aggressive clinical features, whereas overexpression of PRKAB2 markedly inhibited RCC cell proliferation, migration, invasion, tumor growth, and metastasis both and . Mechanistically, PRKAB2 overexpression inhibited mitophagy primarily through two distinct mechanisms. First, PRKAB2 enhanced the binding between LRPPRC and PRKN/parkin, competitively reducing PRKN's interaction with PINK1 and thus suppressing ubiquitin-dependent mitophagy. Second, PRKAB2 promoted AMPK phosphorylation, which in turn suppressed SREBF1/SREBP1-mediated transcriptional activation of , leading to decreased CRLS1 expression and reduced synthesis of cardiolipin, a lipid essential for mitophagy. Importantly, PRKAB2 overexpression significantly restored sensitivity to tyrosine kinase inhibitors (TKIs) in sunitinib-resistant RCC cells. Conversely, forced PRKN expression promoted resistance to these drugs, further implicating mitophagy as a key mechanism underlying TKI resistance. Depmap analysis confirmed the association between increased mitophagy and TKI resistance. Overall, our findings identify PRKAB2 as a critical tumor suppressor in RCC, regulating both protein-protein interactions and lipid metabolism to suppress mitophagy. Targeting PRKAB2-associated pathways may provide a promising therapeutic strategy to enhance treatment efficacy and overcome drug resistance in RCC.: ACACA/ACC1: acetyl-CoA carboxylase alpha; AMPK: AMP-activated protein kinase; ATCC: American Type Culture Collection; ATP5F1A: ATP synthase F1 subunit alpha; BNIP3: BCL2 interacting protein 3; BNIP3L/NIX: BCL2 interacting protein 3 like; BRCA1: BRCA1 DNA repair associated; Cas: CRISPR-associated; CCCP: carbonyl cyanide m-chlorophenyl hydrazone; ccRCC: clear cell renal cell carcinoma; ChIP: chromatin immunoprecipitation; Co-IP: co-immunoprecipitation; COX4I1: cytochrome c oxidase subunit 4I1; CRISPR: clustered regularly interspaced short palindromic repeats; CRLS1: cardiolipin synthase 1; DNM1L/DRP1: dynamin 1 like; DOX: doxorubicin; FUNDC1: FUN14 domain containing 1; HSPA8: heat shock protein family A (Hsp70) member 8; HSPD1: heat shock protein family D (Hsp60) member 1; GO: gene ontology; IHC: immunohistochemistry; IMM: inner mitochondrial membrane; LDLR: low density lipoprotein receptor; m-SREBF1: mature sterol regulatory element binding transcriptional factor 1; LRPPRC: leucine rich pentatricopeptide repeat containing; MAP1LC3B: microtubule associated protein 1 light chain 3 beta; MFN1, mitofusin 1; MFN2: mitofusin 2; MTOR: mechanistic target of rapamycin kinase; OMM: outer mitochondrial membrane; OS: overall survival; PA: phosphatidic acid; PG: phosphatidylglycerol; PGS1: phosphatidylglycerophosphate synthase 1; PINK1: PTEN induced kinase1; PRKAA1/AMPKα1: protein kinase AMP-activated catalytic subunit alpha 1; PRKAA2/AMPKα2: protein kinase AMP-activated catalytic subunit alpha 2; PRKAB1/AMPKβ1: protein kinase AMP-activated catalytic subunit beta 1; PRKAB2/AMPKβ2: protein kinase AMP-activated non-catalytic subunit beta 2; PRKAG1/AMPKγ1: protein kinase AMP-activated non-catalytic subunit gamma 1; PRKN: parkin RBR E3 ubiquitin protein ligase; RCC: renal cell carcinoma; SASA: solvent-accessible surface areas; SUCLG1: succinate-CoA ligase GDP/ADP-forming subunit alpha; TCGA: The Cancer Genome Atlas; TKI: tyrosine kinase inhibitors; UCP1: uncoupling protein 1; ULK1: unc-51 like autophagy activating kinase 1; WCL: whole-cell lysate.
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