{"title":"Advisory Board and Contents","authors":"","doi":"10.1016/S0968-0004(25)00085-4","DOIUrl":"10.1016/S0968-0004(25)00085-4","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages i-ii"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143890552","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":"Subscription and Copyright Information","authors":"","doi":"10.1016/S0968-0004(25)00088-X","DOIUrl":"10.1016/S0968-0004(25)00088-X","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Page e1"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143891170","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":"Cracking the protein compartmentalization code with ProtGPS","authors":"Songtao Ye , Choon Leng So , Danfeng Cai","doi":"10.1016/j.tibs.2025.03.008","DOIUrl":"10.1016/j.tibs.2025.03.008","url":null,"abstract":"<div><div>Cellular protein compartmentalization is essential for function, yet the mechanisms directing proteins to their correct destinations remain unclear. Recently, <span><span>Kilgore, Chinn, Mikhael, and Mitnikov <em>et al</em>.</span><svg><path></path></svg></span> introduced ProtGPS, an artificial intelligence (AI) model that recognizes sequence-encoded localization patterns. ProtGPS predicts condensate-targeting sequences, facilitates peptide design, and identifies pathogenic mutations disrupting protein compartmentalization.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 369-371"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143778711","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":"RNA catalysis moving towards metabolic reactions: progress with ribozyme catalyzed alkyl transfer","authors":"David M.J. Lilley , Lin Huang","doi":"10.1016/j.tibs.2025.01.011","DOIUrl":"10.1016/j.tibs.2025.01.011","url":null,"abstract":"<div><div>The RNA world hypothesis proposes that the early stages of the emergence of life on Earth comprised primitive cells in which RNA acted both to store genetic information and catalyze chemical reactions as RNA enzymes (ribozymes). Most contemporary ribozymes catalyze phosphoryl transfer reactions, but early ribozymes would have been required to catalyze a broader range of metabolic interconversions. None has been found in modern cells, yet ribozymes have been generated by <em>in vitro</em> evolution to catalyze several different chemical reactions, providing proof of principle of RNA-catalyzed metabolism. Recently, several different ribozymes that accelerate methyl or alkyl transfer have been isolated. As we discuss here, one of these, MTR1, uses a remarkably sophisticated catalytic mechanism involving nucleobase-mediated general acid catalysis.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 5","pages":"Pages 417-424"},"PeriodicalIF":11.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584232","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":"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}
Rebecca K. Spangler , Keya Jonnalagadda , Jordan D. Ward , Carrie L. Partch
{"title":"A wrinkle in timers: evolutionary rewiring of conserved biological timekeepers","authors":"Rebecca K. Spangler , Keya Jonnalagadda , Jordan D. Ward , Carrie L. Partch","doi":"10.1016/j.tibs.2025.01.006","DOIUrl":"10.1016/j.tibs.2025.01.006","url":null,"abstract":"<div><div>Biological timing mechanisms are intrinsic to all organisms, orchestrating the temporal coordination of biological events through complex genetic networks. Circadian rhythms and developmental timers utilize distinct timekeeping mechanisms. This review summarizes the molecular basis for circadian rhythms in mammals and <em>Drosophila</em>, and recent work leveraging these clocks to understand temporal regulation in <em>Caenorhabditis elegans</em> development. We describe the evolutionary connections between distinct timing mechanisms and discuss recent insights into the rewiring of core clock components in development. By integrating findings from circadian and developmental studies with biochemical and structural analyses of conserved components, we aim to illuminate the molecular basis of nematode timing mechanisms and highlight broader insights into biological timing across species.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 4","pages":"Pages 344-355"},"PeriodicalIF":11.6,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143424685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}