{"title":"Mps1 kinase functions in mitotic spindle assembly and error correction","authors":"Victor M. Bolanos-Garcia","doi":"10.1016/j.tibs.2025.02.005","DOIUrl":"10.1016/j.tibs.2025.02.005","url":null,"abstract":"<div><div>The protein kinase Mps1 (also known as TTK) is a central component of the mitotic spindle assembly checkpoint (SAC), an essential self-monitoring system of the eukaryotic cell cycle that ensures accurate chromosome segregation by delaying the onset of anaphase until all chromosomes are properly bioriented on the mitotic spindle. Mps1 kinase is an important upstream regulator of the SAC and its recruitment to kinetochores critical for initiating SAC signaling. This review discusses the current understanding of Mps1 essential functions in the SAC, the emerging details of Mps1 role in error correction to safeguard genome stability, and the therapeutic potential of Mps1 inhibition for the treatment of cancer types associated with aberrant SAC signaling and chromosome segregation defects.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 438-453"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143623007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cell surface RNA biology: new roles for RNA binding proteins","authors":"Jennifer Porat , Ryan A. Flynn","doi":"10.1016/j.tibs.2025.03.005","DOIUrl":"10.1016/j.tibs.2025.03.005","url":null,"abstract":"<div><div>Much of our understanding of RNA–protein interactions, and how these interactions shape gene expression and cell state, have come from studies looking at these interactions <em>in vitro</em> or inside the cell. However, recent data demonstrates the presence of extracellular and cell surface-associated RNA such as glycosylated RNA (glycoRNA), suggesting an entirely new environment and cellular topology in which to study RNA–RNA binding protein (RBP) interactions. Here, we explore emerging ideas regarding the landscape of cell surface RNA and RBPs. We also discuss open questions concerning the trafficking and anchoring of RBPs to the cell surface, whether cell surface RBPs (csRBPs) directly interact with cell surface RNA, and how changes in the presentation of csRBPs may drive autoimmune responses.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 402-416"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143741924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Assembling the jigsaw puzzle of life","authors":"Vsevolod V. Gurevich","doi":"10.1016/j.tibs.2025.02.003","DOIUrl":"10.1016/j.tibs.2025.02.003","url":null,"abstract":"<div><div>The cell is a dynamic system where millions of molecules of thousands different kinds act within a complex network with numerous feedback loops. Because we cannot pursue many targets simultaneously, ‘big data’ rarely yield useful leads. Comprehensive models can place the snippets obtained in simplified experimental conditions into a coherent picture.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 374-375"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143655570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Innovations in the electron transport chain fuel archaeal methane metabolism","authors":"Blake E. Downing , Dipti D. Nayak","doi":"10.1016/j.tibs.2025.02.004","DOIUrl":"10.1016/j.tibs.2025.02.004","url":null,"abstract":"<div><div>Methanogenic archaea (or methanogens) produce methane as a by-product of energy metabolism. Strategies for energy conservation differ across methanogens. Some lineages use an electron transport chain (ETC) with an endogenously produced heterodisulfide as an electron acceptor. Of late, culture-independent -omics techniques and genome editing tools have provided new insights into the evolution and function of bioenergetic complexes in methanogen ETCs, which will be the primary focus of this review. We will also discuss how the ETC enhances metabolic flexibility in methanogens and can even permit anaerobic respiration decoupled from methanogenesis. Finally, we expand on how innovations in the ETC might have enabled anaerobic methane oxidation in a closely related group of microorganisms called anaerobic methanotrophic archaea (ANME).</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 425-437"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143708068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"FN3K: the (un)sweetest kinase","authors":"Joyce Ogidigo , Reena Kumari , Viraj R. Sanghvi","doi":"10.1016/j.tibs.2025.03.009","DOIUrl":"10.1016/j.tibs.2025.03.009","url":null,"abstract":"<div><div>Fructosamine 3-kinase (FN3K) mitigates excessive protein glycation by phosphorylating and destabilizing fructosamines, preventing irreversible advanced glycation end-products (AGEs). Recent high-resolution structures of FN3K by <span><span>Garg and On <em>et al</em>.</span><svg><path></path></svg></span> reveal key active-site features, highlighting unique regulatory mechanisms and potential druggable sites and providing a foundation for structure-guided drug development against this target.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 372-373"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143787658","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Histone variants: expanding the epigenetic potential of neurons one amino acid at a time.","authors":"Bradley J Lukasak, Erica Korb","doi":"10.1016/j.tibs.2025.03.015","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.03.015","url":null,"abstract":"<p><p>Replication-independent histone variants play an essential role in postmitotic neurons. Here, we review how the subtle sequence differences of histone variants compared to their canonical counterparts underly neuronal function. We focus on variants H3.3, H2A.Z, H2A.X, macroH2A, and H2BE; all of which contain divergent sequences that coordinate a diverse set of outcomes. In particular, we highlight their role in neuronal development, plasticity, and memory, with an emphasis on how single amino acid changes can mediate these complex functions. Lastly, we comment on an emerging field of study evaluating the link between histone variants and neurological disorders. Future studies of histone variants will be important to furthering our understanding of neuronal function.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143955091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Modifying the modifiers: ubiquitination of ADP-ribosylation in human cells.","authors":"Karla L H Feijs-Žaja, Jonas Siefert, Roko Žaja","doi":"10.1016/j.tibs.2025.03.010","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.03.010","url":null,"abstract":"<p><p>Ubiquitination and ADP-ribosylation are protein post-translational modifications (PTMs) which influence diverse protein properties. In vitro work has indicated that ubiquitin can be ADP-ribosylated and vice versa, ADP-ribose ubiquitinated. An exciting new study by Bejan et al. now demonstrates that ubiquitination of ADP-ribosylated proteins, termed MARUbylation, occurs in human cells.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951822","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Zi-Liang Hu, Hong Wei, Linfeng Sun, Eugenia Russinova
{"title":"Plant steroids on the move: mechanisms of brassinosteroid export.","authors":"Zi-Liang Hu, Hong Wei, Linfeng Sun, Eugenia Russinova","doi":"10.1016/j.tibs.2025.03.003","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.03.003","url":null,"abstract":"<p><p>Brassinosteroids (BRs) are essential plant steroidal hormones that regulate growth and development. The recent discoveries of ATP-binding cassette subfamily B (ABCB) members, ABCB19 and ABCB1, as BR transporters highlight the significance of active export to the apoplast in maintaining BR homeostasis and enabling effective signaling. This review focuses on the latest progress in understanding ABCB-mediated BR transport, with particular attention to the structural and functional characterization of arabidopsis ABCB19 and ABCB1. These findings reveal both conserved and distinct features in substrate recognition and transport mechanisms, providing valuable insights into their roles in hormonal regulation. Additionally, the evolutionary conservation of ABC transporters in mediating steroid-based signaling across biological kingdoms underscores their fundamental biological significance.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143956848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jan-Ole Niemeier, Leticia Prates Roma, Jan Riemer, Markus Schwarzländer, Bruce Morgan
{"title":"Monitoring subcellular NADP redox state with NAPstar biosensors.","authors":"Jan-Ole Niemeier, Leticia Prates Roma, Jan Riemer, Markus Schwarzländer, Bruce Morgan","doi":"10.1016/j.tibs.2025.03.013","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.03.013","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143958878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Mayra A Borrero-Landazabal, Vanessa Linke, Agnieszka Chacinska
{"title":"Lipids: emerging actors in mitochondrial protein import.","authors":"Mayra A Borrero-Landazabal, Vanessa Linke, Agnieszka Chacinska","doi":"10.1016/j.tibs.2025.03.011","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.03.011","url":null,"abstract":"<p><p>Lipids are emerging as functional players in mitochondrial protein import beyond constituting membranes. Cryo-electron microscopy structures of protein translocases such as translocase of the outer membrane (TOM) and insertases such as translocase of the inner membrane (TIM22) link lipids to protein import by suggesting structural and functional roles for lipids in protein translocation and insertion, and for protein insertases in lipid scrambling.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143957113","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}