{"title":"The Leishmania ribosome: more than passive mRNA translating machinery","authors":"","doi":"10.1016/j.tibs.2024.06.008","DOIUrl":"10.1016/j.tibs.2024.06.008","url":null,"abstract":"<div><p><span><span>While the central dogma of molecular biology describes how </span>genetic<span> information flows, gene expression is also affected by epigenetic and epitranscriptomic processes. A recent report by </span></span><span><span>Rajan <em>et al</em></span><svg><path></path></svg></span><em>.</em> demonstrates how pseudouridylation of a <span><span>Leishmania</span></span><span> ribosomal rRNA affects the expression of particular proteins: an example of epitranslatomic control.</span></p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141426003","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":"Migrasome biogenesis: when biochemistry meets biophysics on membranes","authors":"","doi":"10.1016/j.tibs.2024.06.004","DOIUrl":"10.1016/j.tibs.2024.06.004","url":null,"abstract":"<div><p>Migrasomes, newly identified organelles, play crucial roles in intercellular communication, contributing to organ development and angiogenesis. These vesicles, forming on retraction fibers of migrating cells, showcase a sophisticated architecture. Recent research reveals that migrasome biogenesis is a complicated and highly regulated process. This review summarizes the mechanisms governing migrasome formation, proposing a model in which biogenesis is understood through the lens of membrane microdomain assembly. It underscores the critical interplay between biochemistry and biophysics. The biogenesis unfolds in three distinct stages: nucleation, maturation, and expansion, each characterized by unique morphological, biochemical, and biophysical features. We also explore the broader implications of migrasome research in membrane biology and outline key unanswered questions that represent important directions for future investigation.</p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141465328","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":"Cellular oxidants and the proteostasis network: balance between activation and destruction","authors":"","doi":"10.1016/j.tibs.2024.07.001","DOIUrl":"10.1016/j.tibs.2024.07.001","url":null,"abstract":"<div><p>Loss of protein homeostasis (proteostasis) is a common hallmark of aging and age-associated diseases. Considered as the guardian of proteostasis, the proteostasis network (PN) acts to preserve the functionality of proteins during their lifetime. However, its activity declines with age, leading to disease manifestation. While reactive oxygen species (ROS) were traditionally considered culprits in this process, recent research challenges this view. While harmful at high concentrations, moderate ROS levels protect the cell against age-mediated onset of proteotoxicity by activating molecular chaperones, stress response pathways, and autophagy. This review explores the nuanced roles of ROS in proteostasis and discusses the most recent findings regarding the redox regulation of the PN and its potential in extending healthspan and delaying age-related pathologies.</p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0968000424001646/pdfft?md5=e438983700d0e46168c3bfae96cab77d&pid=1-s2.0-S0968000424001646-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142015999","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}
{"title":"IUBMB Trainee Initiative: supporting emerging biochemists and molecular biologists around the world","authors":"","doi":"10.1016/j.tibs.2024.07.004","DOIUrl":"10.1016/j.tibs.2024.07.004","url":null,"abstract":"<div><p>The International Union of Biochemistry and Molecular Biology (IUBMB) Trainee Initiative aims to identify challenges experienced by biochemistry and molecular biology trainees and create programming to foster their growth and development as the next generation of scientists. Here, we highlight resources and events developed by the Trainee Initiative in their endeavor to support trainees around the world.</p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0968000424001816/pdfft?md5=1766f2b5945a5294a72bfa46625178ac&pid=1-s2.0-S0968000424001816-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142144854","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}
{"title":"Structural transitions modulate the chaperone activities of Grp94","authors":"","doi":"10.1016/j.tibs.2024.06.007","DOIUrl":"10.1016/j.tibs.2024.06.007","url":null,"abstract":"<div><p>A recent study by <span><span>Amankwah <em>et al.</em></span><svg><path></path></svg></span><span> reports how co-chaperone proteins and ATP hydrolysis<span><span> fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 </span>paralog Grp94.</span></span></p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141436531","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":"Beyond the bench: motivations and aspirations of the IUBMB Trainee Initiative Leadership Committee","authors":"","doi":"10.1016/j.tibs.2024.07.003","DOIUrl":"10.1016/j.tibs.2024.07.003","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0968000424001804/pdfft?md5=7afd34d52e497ed766019a7d1d8b0473&pid=1-s2.0-S0968000424001804-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142144853","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}
{"title":"Versatile JMJD proteins: juggling histones and much more","authors":"","doi":"10.1016/j.tibs.2024.06.009","DOIUrl":"10.1016/j.tibs.2024.06.009","url":null,"abstract":"<div><p>Jumonji C domain-containing (JMJD) proteins are found in bacteria, fungi, animals, and plants. They belong to the 2-oxoglutarate-dependent oxygenase superfamily and are endowed with various enzymatic activities, including demethylation of histones and hydroxylation of non-histone proteins. Many JMJD proteins are involved in the epigenetic control of gene expression, yet they also modulate a myriad other cellular processes. In this review we focus on the 33 human JMJD proteins and their established and controversial catalytic properties, survey their epigenetic and non-epigenetic functions, emphasize their contribution to sex-specific disease differences, and highlight how they sense metabolic changes. All this underlines not only their key roles in development and homeostasis, but also that JMJD proteins are destined to become drug targets in multiple diseases.</p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141454486","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(24)00200-7","DOIUrl":"10.1016/S0968-0004(24)00200-7","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142157604","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":"Advisory Board and Contents","authors":"","doi":"10.1016/S0968-0004(24)00197-X","DOIUrl":"10.1016/S0968-0004(24)00197-X","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S096800042400197X/pdfft?md5=4cf0e61b464c1e32c0d7234ffa2149e3&pid=1-s2.0-S096800042400197X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142157854","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}
{"title":"Functional implications of fumarate-induced cysteine succination","authors":"","doi":"10.1016/j.tibs.2024.05.003","DOIUrl":"10.1016/j.tibs.2024.05.003","url":null,"abstract":"<div><p>Mutations in metabolic enzymes are associated with hereditary and sporadic forms of cancer. For example, loss-of-function mutations affecting fumarate hydratase (FH), the tricarboxylic acid (TCA) cycle enzyme, result in the accumulation of millimolar levels of fumarate that cause an aggressive form of kidney cancer. A distinct feature of fumarate is its ability to spontaneously react with thiol groups of cysteines in a chemical reaction termed succination. Although succination of a few proteins has been causally implicated in the molecular features of FH-deficient cancers, the stoichiometry, wider functional consequences, and contribution of succination to disease development remain largely unexplored. We discuss the functional implications of fumarate-induced succination in FH-deficient cells, the available methodologies, and the current challenges in studying this post-translational modification.</p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":null,"pages":null},"PeriodicalIF":11.6,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0968000424001130/pdfft?md5=df3dc6aac16d13e59cc8af993548abc8&pid=1-s2.0-S0968000424001130-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141320369","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}