Biochemical Society Transactions[JOURNAL]
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200 papers
Structure and function of periplasmic nitrate reductase.
Mongkonpruthangkoon C, Giri NC, Basu P
Biochem Soc Trans · 2026 Jun · PMID 42206606 · Full text
Nitrate reductases are molybdenum cofactor (Moco)-containing enzymes that reduce nitrate to nitrite, the first step in assimilatory and dissimilatory nitrate reduction to ammonia, and in denitrification. Nitrate reductas...
Nitrate reductases are molybdenum cofactor (Moco)-containing enzymes that reduce nitrate to nitrite, the first step in assimilatory and dissimilatory nitrate reduction to ammonia, and in denitrification. Nitrate reductases are divided into four groups; this review will focus on periplasmic nitrate reductase (Nap), discussing the available structures of NapA in the context of other members of the DMSO reductase family. The mechanism and the roles of a specific amino acid residue are also discussed.
Dissecting conserved molecular mechanisms of biological toxin activity through CRISPR screening.
Waller MA, D'Araujo TY, Denes CE … +1 more , Neely GG
Biochem Soc Trans · 2026 Jun · PMID 42206605 · Full text
Toxins, substances that are produced by living organisms with the potential to cause harm, demonstrate great diversity in their structure, function, and origin. Though some toxins have been repurposed for use as novel th...
Toxins, substances that are produced by living organisms with the potential to cause harm, demonstrate great diversity in their structure, function, and origin. Though some toxins have been repurposed for use as novel therapeutics, research tools, or for application in agriculture, the mechanism of action for many toxins remains uncharacterised. Pooled CRISPR screens offer a high-throughput and unbiased method for rapid annotation of the host cell genome and identification of factors mediating or modifying intoxication. In this review, we provide a brief overview of CRISPR screening before detailing how screens have been used to characterise toxins from various biological kingdoms. We highlight certain cell entry factors and intracellular processes as conserved targets of various toxins. Finally, we highlight limitations in the methods of CRISPR screens used thus far and make recommendations as to how screen design can be modified to more completely characterise toxin activity and elucidate systemic effects of intoxication.
RNA-binding protein hnRNPK: a multifunctional regulator of skeletal muscle biology and disease.
Ren K, Zhou K, An Y … +6 more , Cheng X, Meng T, Li C, Xu H, Zhang P, Xu Y
Biochem Soc Trans · 2026 May · PMID 42165226 · Full text
Heterogeneous nuclear ribonucleoprotein K (hnRNPK) is a highly conserved, multifunctional DNA/RNA-binding protein that regulates gene expression at both transcriptional and post-transcriptional levels. In skeletal muscle...
Heterogeneous nuclear ribonucleoprotein K (hnRNPK) is a highly conserved, multifunctional DNA/RNA-binding protein that regulates gene expression at both transcriptional and post-transcriptional levels. In skeletal muscle, hnRNPK is essential for development, regeneration, and homeostasis, influencing satellite cell activation, myoblast proliferation and differentiation, and myofiber maturation. Its dysregulation is linked to muscle atrophy, degenerative diseases, and impaired regeneration. This review summarizes current knowledge of hnRNPK's molecular structure, subcellular localization and dynamics, and interactions with nucleic acids and proteins. We highlight its roles in myogenic differentiation, gene expression control, signaling pathway cross-talk, and skeletal muscle development. We also discuss the potential of hnRNPK as a diagnostic biomarker and therapeutic target in muscle disorders, and outline key directions for future research to resolve outstanding questions about its complex regulatory functions. Together, these insights provide a framework for advancing muscle biology and improving the management of muscle-related diseases.
G0 or no-G0: phosphatase control of quiescence and cell cycle entry.
Robinson EA, Barr AR
Biochem Soc Trans · 2026 May · PMID 42165225 · Full text
During each cell cycle, cells must decide whether to continue to proliferate or to exit the cell cycle into a reversible arrest state, known as quiescence, or G0. This decision must be highly regulated to ensure proper t...
During each cell cycle, cells must decide whether to continue to proliferate or to exit the cell cycle into a reversible arrest state, known as quiescence, or G0. This decision must be highly regulated to ensure proper tissue homeostasis. Studies on kinase-driven signalling pathways that regulate this decision point have dominated the field, and the role of phosphatases remains comparatively underexplored, yet the role of phosphatases is vitally important in signal transduction. In the present review, we examine how phosphatases contribute to the regulation of quiescence in mammalian cells across three stages: entry into quiescence, maintenance of the quiescent state, and quiescence exit into the cell cycle. We discuss how phosphatases counteract mitogenic signalling pathways, including MAPK/ERK and PI3K-AKT-mTOR, and maintain low cyclin-dependent kinase (CDK) activity through dephosphorylation of key cell cycle regulators, such as the retinoblastoma family proteins and CDK inhibitors. Finally, we highlight emerging evidence that dynamic regulation of phosphatase activity shapes the transition from quiescence back into proliferation. Understanding how phosphatases regulate the reversible nature of cell cycle arrest is important for understanding how tissues maintain homeostasis and how dysregulation of quiescence contributes to disease, including cancer.
Direct or indirect: the crucial role of N-palmitate in hedgehog signaling.
Puschmann J, Grobe K
Biochem Soc Trans · 2026 May · PMID 42138130 · Full text
During development, cells use concentration gradients of soluble signaling molecules, called morphogens, to determine their position within tissues and adopt the correct identity. Hedgehog (Hh) morphogens are a key but a...
During development, cells use concentration gradients of soluble signaling molecules, called morphogens, to determine their position within tissues and adopt the correct identity. Hedgehog (Hh) morphogens are a key but also unusual example of gradient formation, because their diffusion away from their origin to direct growth and patterning is first prevented by their dual N- and C-terminal lipidation by palmitate and cholesterol. These lipids associate the Hhs with the plasma membrane of the cells that produce them. Later, however, both lipids participate in the spatiotemporal release of Hh by accessory proteins and maintain Hh biofunction in vivo, either directly or indirectly. The present study explores these two mechanistic possibilities, focusing on the central role of N-palmitate in Hh-regulated development in both vertebrates and invertebrates.
Pro-inflammatory cytokine-driven molecular signaling in skeletal muscle during cancer cachexia.
Pati B, Nandy N, Bindhani BK … +1 more , Bal NC
Biochem Soc Trans · 2026 May · PMID 42138129 · Full text
Cancer cachexia is a multifactorial syndrome characterized by the progressive loss of muscle and fat, commonly observed among patients with cancer. It is very distinct from other skeletal muscle wasting such as sarcopeni...
Cancer cachexia is a multifactorial syndrome characterized by the progressive loss of muscle and fat, commonly observed among patients with cancer. It is very distinct from other skeletal muscle wasting such as sarcopenia and malnutrition and is known to reduce cancer treatment effectiveness. Cachexia progression is driven by a combination of factors, including hormonal dysregulation, anorexia, tumor-derived catabolic factors (in cancer cachexia), and systemic or muscular inflammation, all of which worsen overall muscle health. In this review, we will probe the role of pro-inflammatory cytokines, such as IL-6, IFN-γ, TNF-α, TGF-β, IL-1β, and IL-8, in driving the systemic inflammation and disruption of muscle metabolic homeostasis that support the development of cachexia. These cytokines may be produced from various organs, including the adipose depots that contribute to muscle wasting and metabolic dysfunction by disrupting the equilibrium between anabolic and catabolic processes. The ubiquitin-proteasome system, NF-κB, and JAK/STAT3 are important molecular pathways that mediate cytokine-induced catabolic signaling. The review further analyzes the context-dependent dual functions of these cytokines and the molecular mechanisms underlying the loss of their regulatory control during cancer progression. The limited success of current therapeutic approaches for cancer cachexia highlights the urgent need for evaluation of more targetable mechanisms for the treatments. Here, one of our main objectives is to probe whether suppression of pro-inflammatory cytokine signaling and activation of anti-inflammatory pathways can be utilized to modulate the tumor microenvironment, thereby countering cancer cachexia.
Structural insights into HRI kinase activity and inhibition.
Cao M, Masson GR
Biochem Soc Trans · 2026 May · PMID 42138128 · Full text
Haem-regulated inhibitor (HRI) is emerging as a potential therapeutic target in several disease areas, including cancers such as multiple myeloma and neurodegenerative disease. As one of four related mammalian kinases th...
Haem-regulated inhibitor (HRI) is emerging as a potential therapeutic target in several disease areas, including cancers such as multiple myeloma and neurodegenerative disease. As one of four related mammalian kinases that phosphorylate the mRNA translation machinery substrate eIF2α, it has a central role in sensing several disparate proteotoxic stresses and preventing subsequent rounds of protein production. In this review, we will examine the latest research on the structural and molecular basis of HRI inhibition and activation, examining both regulatory biological interactions with proteins and cofactors. What emerges is that despite almost 75 years since the first identification of HRI, we still know remarkably little about how this kinase functions and is regulated.
Mechanistic insight into the oxidative degradation of monoclonal antibodies: relevance to developability and the design of stable pharmaceutical formulations.
Schöneich C
Biochem Soc Trans · 2026 May · PMID 42132105 · Full text
Oxidation represents a key pathway for the chemical degradation of therapeutic monoclonal antibodies (mAbs), and chemical liabilities such as amino acid residue oxidation are an integral part of developability studies. M...
Oxidation represents a key pathway for the chemical degradation of therapeutic monoclonal antibodies (mAbs), and chemical liabilities such as amino acid residue oxidation are an integral part of developability studies. Mechanistically, oxidation reactions in formulations of therapeutic mAbs are frequently not well understood, as critical information such as the nature of the oxidant(s) is frequently lacking. This brief review summarizes recent screening and developability studies of therapeutic proteins specifically focusing on oxidative liabilities and discusses these data in view of mechanistic and complementary analytical information on the oxidation of amino acid residues in specific protein sequences.
Membrane protein structure and dynamics probed by MicroED.
Paz O, Gonen T
Biochem Soc Trans · 2026 May · PMID 42101423 · Full text
Membrane proteins are essential to cellular signaling, transport, and homeostasis, yet their amphipathic nature, dependence on lipids or detergents, and typically difficult expression and purification make them difficult...
Membrane proteins are essential to cellular signaling, transport, and homeostasis, yet their amphipathic nature, dependence on lipids or detergents, and typically difficult expression and purification make them difficult targets for structural methods such as X-ray crystallography. Moreover, most membrane proteins in the human proteome are too small for investigation by single-particle electron cryomicroscopy methods. Microcrystal Electron Diffraction (MicroED) has emerged as a powerful method for overcoming these barriers, allowing structure determination from nanocrystals of membrane proteins embedded in the near-native environment of the lipid membrane. In the present review, we discuss how recent improvements in MicroED, such as focused ion-beam milling and high-throughput data collection approaches, facilitate structure determination and investigation of protein dynamics. We focus on applications involving junction-forming proteins, G protein-coupled receptors, and ion channels, where MicroED has revealed physiologically relevant assemblies, lipid interactions, and transient functional states that were not attainable by other structural biology methods.
TAM receptor tyrosine kinases as potential mediators of the non-lytic spread of non-enveloped viruses.
Moran SJ, Starbird CA
Biochem Soc Trans · 2026 May · PMID 42101422 · Full text
Tyro3, Axl, and Mer are receptor tyrosine kinases that comprise the TAM receptor family. These receptors, originally identified as orphan receptors, do not bind growth factors but rather ligands that can facilitate proce...
Tyro3, Axl, and Mer are receptor tyrosine kinases that comprise the TAM receptor family. These receptors, originally identified as orphan receptors, do not bind growth factors but rather ligands that can facilitate processes such as phagocytosis and dampening the innate inflammatory immune response. Enveloped viruses can hijack TAM receptors for viral entry through the fairly well-established mechanism of apoptotic mimicry. This mechanism involves 'tricking' the targeted host cell into endocytosing the virus through binding to exposed phosphatidylserine in the viral lipid bilayer envelope. While enveloped viruses utilize apoptotic mimicry for entry, it remains unclear how non-enveloped viruses enter the host cell through phosphatidylserine receptors such as TAM receptors. There is evidence that non-enveloped viruses can usurp host cell signaling pathways to cloak their particles in membranes, creating 'quasi-enveloped' viruses that enter the host through a sort of 'faux apoptotic mimicry.' These quasi-enveloped viruses can spread through non-lytic mechanisms to evade the host immune response and deliver virus particles to the targeted host cell. With the present review, we evaluate increasing evidence that TAM receptors may play a role in this process through their ability to indiscriminately bind phosphatidylserine in membranes, leading to the internalization of non-enveloped viruses packaged within phosphatidylserine-enriched extracellular vesicles.
Native mass spectrometry meets X-rays for the elucidation of protein structures.
Kierspel T, de Santis E, Schamoni-Kast K … +4 more , Blanchet C, Marklund EG, Caleman C, Uetrecht C
Biochem Soc Trans · 2026 May · PMID 42101421 · Full text
Small-angle X-ray scattering (SAXS) is a powerful and widely used technique for structural biology, providing information about solution structures, i.e., without the need for crystallization or cryogenic conditions. How...
Small-angle X-ray scattering (SAXS) is a powerful and widely used technique for structural biology, providing information about solution structures, i.e., without the need for crystallization or cryogenic conditions. However, its applicability is limited in cases where sample heterogeneity, conformational mixtures, or aggregation are present. While modern BioSAXS routinely employs inline purification (e.g., SEC-SAXS) to address heterogeneity, gas-phase SAXS, enabled by native mass spectrometry as a sample delivery method, offers an even higher degree of population selectivity by providing well-defined and mass-selected ion populations. The principal challenge of this approach is the inherently low particle density in the gas phase. In the present overview, we present simulations of gas-phase SAXS viral nonstructural proteins and capsids and compare them against diffraction patterns from prototypical GroEL. We evaluate the expected scattering signal under experimentally realistic conditions and discuss potential implementations and use cases at both synchrotron radiation sources and X-ray free-electron lasers, thereby outlining regimes in which gas-phase SAXS may become a viable complementary tool for structural studies.
Rho GTPases in cancer resistance: mechanisms, vulnerabilities, and therapeutic opportunities.
Beaudin A, Lefrançois P, Laurin M
Biochem Soc Trans · 2026 May · PMID 42093646 · Full text
Intrinsic and adaptive resistance to therapy remain major barriers to effective cancer treatment. Diverse resistance mechanisms, including epithelial-mesenchymal transition, enhanced tolerance to DNA damage, impaired cel...
Intrinsic and adaptive resistance to therapy remain major barriers to effective cancer treatment. Diverse resistance mechanisms, including epithelial-mesenchymal transition, enhanced tolerance to DNA damage, impaired cell death pathways, metabolic reprogramming, and cues from the tumour microenvironment, are increasingly recognised as being tightly integrated with Rho GTPase signalling networks. Accumulating evidence positions these pathways as central regulators of therapeutic resistance across multiple cancer types. In this review, we synthesise recent experimental findings linking Rho GTPase-mediated signalling to therapy resistance and evaluate emerging strategies aimed at targeting these signalling axes. We critically examine the translational readiness of approaches that directly inhibit Rho GTPases, disrupt downstream effector pathways, or modulate canonical regulators such as RhoGEFs and RhoGAPs, and discuss the key challenges and opportunities associated with their clinical deployment. Collectively, these insights highlight the therapeutic potential of targeting Rho GTPase signalling as a foundation for next-generation cancer treatments.
Lipid transport mechanisms in human ABCA family transporters: a structural perspective.
Dolai S, Alam A
Biochem Soc Trans · 2026 May · PMID 42093645 · Full text
ATP-binding cassette (ABC) transporters are essential membrane proteins that couple ATP hydrolysis to move diverse substrates across lipid bilayers through large-scale conformational changes. In humans, 48 ABC transporte...
ATP-binding cassette (ABC) transporters are essential membrane proteins that couple ATP hydrolysis to move diverse substrates across lipid bilayers through large-scale conformational changes. In humans, 48 ABC transporters span seven subfamilies (A-G); within these, the ABCA subfamily mediates cellular lipid handling in contexts ranging from neural function to pulmonary surfactant production, and its dysfunction contributes to human disease from cardiovascular disorders to Alzheimer's. These diverse physiological roles all depend on precise lipid translocation within or across membrane systems, a shared principle that is often underemphasized in broad "lipid-transporter" classifications. This review summarizes the structural landscape of the ABCA family and re-examines the mechanistic insights that have emerged. We compare and contrast transport models derived from detergent-solubilized and lipid-embedded structures, with particular emphasis on lipid-embedded ABCA7, which supports a membrane-integrated mechanism in which the bilayer itself contributes to the transport pathway. We highlight shared rigid-body transitions, outline open questions surrounding transport directionality and protein-lipid coupling, and suggest that future models should treat the membrane not merely as a passive scaffold but as an integral component of the transport mechanism, while recognizing that membrane-integrated behavior is currently established structurally only for ABCA7 and remains a working hypothesis for other family members.
MGRN1 in development and disease: a unifying view of a versatile membrane-tethered E3 ubiquitin ligase.
Riglos A, Gunn TM, Kong JH
Biochem Soc Trans · 2026 May · PMID 42089370 · Full text
Mahogunin Ring Finger 1 (MGRN1) is a multifunctional E3 ubiquitin ligase with broad biological significance and belongs to a small group of membrane-tethered E3s capable of regulating signaling receptors at the plasma me...
Mahogunin Ring Finger 1 (MGRN1) is a multifunctional E3 ubiquitin ligase with broad biological significance and belongs to a small group of membrane-tethered E3s capable of regulating signaling receptors at the plasma membrane. Studies in mice first revealed its physiological importance, as loss of Mgrn1 leads to a wide range of phenotypes, including abnormal pigmentation, congenital malformations, and neurodegeneration. Remarkably, MGRN1 localizes to multiple cellular compartments, including the plasma membrane, mitochondria, nucleus, and endo-lysosomal pathway. MGRN1 is also involved in several cellular processes, including receptor regulation, protein homeostasis, and mitochondrial maintenance. While studies have emphasized the importance of MGRN1, it has been difficult to define unifying principles governing its function. In the present review, we summarize and integrate published findings to develop a clearer picture of MGRN1's roles, focusing on phenotypes observed in mouse models and the signaling pathways MGRN1 regulates. We propose shared mechanistic themes that reconcile the functional diversity of this unique E3 ligase, highlight gaps in the current literature, and identify areas for further investigation to better understand MGRN1's role in disease and evaluate its potential relevance for targeted protein degradation strategies.
Unraveling new functions of the Ca2+ sensor STIM1 in cell signaling.
Sanchez-Lopez I, Orantos-Aguilera Y, Lopez-Guerrero AM … +2 more , Pozo-Guisado E, Martin-Romero FJ
Biochem Soc Trans · 2026 May · PMID 42089369 · Full text
Calcium (Ca2+) signaling is a fundamental regulator of virtually all aspects of eukaryotic cell physiology, including gene expression, secretion, metabolism, motility, and cell fate decisions. The spatial and temporal co...
Calcium (Ca2+) signaling is a fundamental regulator of virtually all aspects of eukaryotic cell physiology, including gene expression, secretion, metabolism, motility, and cell fate decisions. The spatial and temporal control of cytosolic Ca2+ signals relies on a coordinated interplay between intracellular Ca2+ stores and plasma membrane (PM) Ca2+ channels. A critical advance in this field over the past two decades was the molecular identification of stromal interaction molecule 1 (STIM1) as the long-sought Ca2+ sensor that couples depletion of endoplasmic reticulum Ca2+ stores to Ca2+ influx across the PM. STIM1 has been established as a core component of store-operated Ca2+ entry, acting through direct activation of ORAI Ca2+ channels. However, accumulating evidence now indicates that STIM1 functions extend beyond this canonical role. STIM1 participates in the regulation of multiple classes of ion channels, contributes to the organization of membrane contact sites, and acts as a signaling scaffold influencing cellular processes independently of classical store depletion. This review summarizes the discovery and canonical functions of STIM1 and focuses on its emerging non-canonical roles, highlighting how STIM1 has evolved from an ER Ca2+ sensor into a multifunctional signaling hub.
Mimetics of in-cell and subcellular crowding and solvation for protein folding.
Knab E, Tahir U, Davis CM
Biochem Soc Trans · 2026 Apr · PMID 42057658 · Full text
Historically, fundamental principles of protein folding were extracted from dilute in vitro experiments that disregarded the complexity of the cell interior. It is now well-established that the cellular environment modul...
Historically, fundamental principles of protein folding were extracted from dilute in vitro experiments that disregarded the complexity of the cell interior. It is now well-established that the cellular environment modulates protein behaviors. Discrepancies between protein properties measured in vitro and in-cell can be disentangled using mimetics that are designed to reproduce cellular interactions in vitro, steric crowding interactions and non-steric sticking interactions. Here, we review recent advances in the development and application of cellular mimetics of in-cell protein folding, with a focus on replicating diverse cell types and cellular compartments. Steric crowding interactions are typically mimicked using inert polymers; coupling these with giant unilamellar vesicles or phase separation allows for the creation of a cell- or organelle-like environment. Mimetics of non-steric chemical interactions must incorporate features of the chemical environment being mimicked. These range from buffers containing physiological concentrations of salt and small molecules to dilute lysates derived from the relevant cell type and/or organelle. Such mimetics of steric and non-steric interactions have greatly aided our understanding of in-cell protein folding. Mimetics can further approach biological accuracy through mixtures that simultaneously account for steric and non-steric interactions. Mimetic mixtures are important because they provide a convenient and cost-effective means to predict protein behavior in diverse cellular environments, which may benefit high-throughput applications, such as screening therapeutic candidates or training machine learning-based in-cell protein structure prediction models.
How intrinsically disordered regions shape the function of CREB-binding protein.
Gilbert G, Bose DA
Biochem Soc Trans · 2026 Apr · PMID 42057657 · Full text
CREB-binding protein (CBP) is a histone acetyltransferase and transcriptional co-activator that operates across the genome at cis-regulatory elements (CREs) to regulate gene expression. Comprising the majority of the pro...
CREB-binding protein (CBP) is a histone acetyltransferase and transcriptional co-activator that operates across the genome at cis-regulatory elements (CREs) to regulate gene expression. Comprising the majority of the protein, CBP has intrinsically disordered regions (IDRs) that separate its folded domains. Whilst previously regarded as passive linkers, active roles for these IDRs within CBP are beginning to be uncovered. Firstly, the flexibility afforded by these regions and the presence of binding motifs within them establish CBP as an interaction specialist that is able to interact with many binding partners at diverse CREs. In addition, the IDRs of CBP allow it to undergo liquid-liquid phase separation, forming condensates with emerging roles in transcription. Finally, an IDR within CBP performs an autoregulatory function that makes histone acetyltransferase activity sensitive to changing conditions within the cell. To build a comprehensive understanding of CBP function going forwards, it will be necessary to consider the contributions of the IDRs in addition to the structured domains of CBP and how these are integrated for the regulation of this key transcriptional protein.
The amplification of α-synuclein amyloid fibrils.
Buell AK
Biochem Soc Trans · 2026 Apr · PMID 42057656 · Full text
Amyloid fibrils formed by α-synuclein are a hallmark of a range of neurodegenerative diseases, notably Parkinson's disease, multiple system atrophy (MSA), and dementia with Lewy bodies, collectively known as synucleinopa...
Amyloid fibrils formed by α-synuclein are a hallmark of a range of neurodegenerative diseases, notably Parkinson's disease, multiple system atrophy (MSA), and dementia with Lewy bodies, collectively known as synucleinopathies. Recent years have seen an increasing understanding of the structural architecture and diversity of α-synuclein amyloid fibrils. Furthermore, our mechanistic understanding of the formation of these structures has also experienced significant progress. Here, I provide a concise overview of the current state of knowledge of how α-synuclein amyloid fibrils can be amplified, i.e., increase in number. The main emphasis is thereby on the process of secondary nucleation, i.e., the generation of new amyloid fibrils catalyzed by existing fibrils. A detailed understanding of fibril amplification is relevant in the context of the spread of pathology in the central nervous system of synucleinopathy patients. In addition, it can also be exploited in the framework of diagnostic approaches collectively known as seed amplification assays (SAAs). In such assays, the minute quantities of α-synuclein fibrils present in biological fluids are amplified and possibly quantified for disease diagnostics.
Glutamine metabolic enzymes: to filament or not to filament?
Machado RAC, Rosa E Silva I, Fontes-Milz T … +4 more , Chang-Halabi Y, Vargas JA, Ambrosio ALB, Dias SMG
Biochem Soc Trans · 2026 Apr · PMID 42051118 · Full text
The self-assembly of metabolic enzymes into filaments and other supramolecular structures is well-documented in bacteria and yeast but remains largely unexplored in mammalian cells. Enzyme filamentation is thought to pla...
The self-assembly of metabolic enzymes into filaments and other supramolecular structures is well-documented in bacteria and yeast but remains largely unexplored in mammalian cells. Enzyme filamentation is thought to play a crucial role in regulating metabolic networks by modulating enzymatic activity in response to cellular demands. Studies in yeast suggest that filament-forming enzymes are often positioned at key junctions of metabolic pathways, enabling dynamic activation or inactivation during growth or stress and directing metabolic flux accordingly. While this mechanism appears to be broadly conserved across species, the structural and functional characterization of human homologs of filamentous enzymes remains limited. In the present review, we focus on the glutamine metabolic pathway, highlighting enzymes known to form large self-assemblies in cells and examining the few cases where structural insights are available. Finally, we discuss the broader implications of metabolic enzyme filamentation in mammalian cells, underscoring its potential as an emerging area of research.
Emerging concepts of reactive oxygen species functions in plants.
Foyer CH
Biochem Soc Trans · 2026 Apr · PMID 42051117 · Full text
Reactive oxygen species (ROS) are ubiquitous signalling molecules that serve to integrate developmental, metabolic and stress signals to shape adaptive outcomes, linking energy metabolism to plant physiology, growth and...
Reactive oxygen species (ROS) are ubiquitous signalling molecules that serve to integrate developmental, metabolic and stress signals to shape adaptive outcomes, linking energy metabolism to plant physiology, growth and stress resilience in a changing world. Resolving the factors and mechanisms involved in ROS-mediated control has proved to be far from trivial, not least because ROS are produced by every compartment of plant cells, serving multiple functions with numerous points of reciprocal control between phytohormones and other signalling pathways. While many enzymes produce hydrogen peroxide (H2O2) directly, other ROS sources such as respiratory burst oxidase homologues (RBOH) produce superoxide as a primary product. Key questions remain concerning the respective roles of superoxide and H2O2 in redox regulation of plant growth, development and defence, and how plant cells can differentiate between ROS produced in different cellular compartments. One solution concerns cysteine (Cys) molecular switches, which are specialised protein thiols that operate as highly sensitive ROS sensors in different locations, transducing changes in oxidation status to the nucleus and facilitating functional changes in protein activity, structure, and localisation. In addition, it is likely that the localisation and positions of many redox proteins, such as catalase and RBOH, are not as fixed as initially proposed, allowing plasticity of function in different compartments. This review discusses current concepts in plant ROS biology, highlighting novel aspects that permeate every aspect of plant biology.
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