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UPS-dependent strategies of protein quality control degradation 依赖 UPS 的蛋白质质量控制降解策略。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-10-01 DOI: 10.1016/j.tibs.2024.06.006
{"title":"UPS-dependent strategies of protein quality control degradation","authors":"","doi":"10.1016/j.tibs.2024.06.006","DOIUrl":"10.1016/j.tibs.2024.06.006","url":null,"abstract":"<div><div>The degradation of damaged proteins is critical for tissue integrity and organismal health because damaged proteins have a high propensity to form aggregates. E3 ubiquitin ligases are key regulators of protein quality control (PQC) and mediate the selective degradation of damaged proteins, a process termed ‘PQC degradation’ (PQCD). The degradation signals (degrons) that trigger PQCD are based on hydrophobic sites that are normally buried within the native protein structure. However, an open question is how PQCD-specialized E3 ligases distinguish between transiently misfolded proteins, which can be efficiently refolded, and permanently damaged proteins, which must be degraded. While significant progress has been made in characterizing degradation determinants, understanding the key regulatory signals of cellular and organismal PQCD pathways remains a challenge.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"49 10","pages":"Pages 859-874"},"PeriodicalIF":11.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141465329","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}
引用次数: 0
Enzoology: understanding enzyme interactions and epistasis in the cell 酶学：了解细胞中的酶相互作用和表观遗传。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-10-01 DOI: 10.1016/j.tibs.2024.07.002
Andrew Savinov
{"title":"Enzoology: understanding enzyme interactions and epistasis in the cell","authors":"Andrew Savinov","doi":"10.1016/j.tibs.2024.07.002","DOIUrl":"10.1016/j.tibs.2024.07.002","url":null,"abstract":"<div><div>Recent work from <span><span>Nguyen <em>et al</em>.</span><svg><path></path></svg></span><span><span><span> unveils massively parallel measurements of epistatic interactions between two enzymes, </span>dihydrofolate reductase and </span>thymidylate synthase, in their natural cellular context. Almost 3000 mutations of DHFR in three TYMS backgrounds reveal a complex interaction network. The authors capture much of this complexity using a simple model.</span></div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"49 10","pages":"Pages 841-842"},"PeriodicalIF":11.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141756458","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}
引用次数: 0
Catchers of folding gone awry: a tale of small heat shock proteins. 折叠出错的捕手：小型热休克蛋白的故事。
IF 13.8 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-12 DOI: 10.1016/j.tibs.2024.08.003
Carsten Peters,Martin Haslbeck,Johannes Buchner
{"title":"Catchers of folding gone awry: a tale of small heat shock proteins.","authors":"Carsten Peters,Martin Haslbeck,Johannes Buchner","doi":"10.1016/j.tibs.2024.08.003","DOIUrl":"https://doi.org/10.1016/j.tibs.2024.08.003","url":null,"abstract":"Small heat shock proteins (sHsps) are an important part of the cellular system maintaining protein homeostasis under physiological and stress conditions. As molecular chaperones, they form complexes with different non-native proteins in an ATP-independent manner. Many sHsps populate ensembles of energetically similar but different-sized oligomers. Regulation of chaperone activity occurs by changing the equilibrium of these ensembles. This makes sHsps a versatile and adaptive system for trapping non-native proteins in complexes, allowing recycling with the help of ATP-dependent chaperones. In this review, we discuss progress in our understanding of the structural principles of sHsp oligomers and their functional principles, as well as their roles in aging and eye lens transparency.","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"33 1","pages":""},"PeriodicalIF":13.8,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142267666","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}
引用次数: 0
The Leishmania ribosome: more than passive mRNA translating machinery 利什曼原虫核糖体：不只是被动的 mRNA 翻译机器。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/j.tibs.2024.06.008
{"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":"49 9","pages":"Pages 754-756"},"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}
引用次数: 0
Migrasome biogenesis: when biochemistry meets biophysics on membranes 移行体的生物发生：当生物化学与生物物理学在膜上相遇。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/j.tibs.2024.06.004
{"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":"49 9","pages":"Pages 829-840"},"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}
引用次数: 0
Cellular oxidants and the proteostasis network: balance between activation and destruction 细胞氧化剂与蛋白稳态网络：激活与破坏之间的平衡。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/j.tibs.2024.07.001
Agnes Ulfig , Ursula Jakob
{"title":"Cellular oxidants and the proteostasis network: balance between activation and destruction","authors":"Agnes Ulfig ,&nbsp;Ursula Jakob","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":"49 9","pages":"Pages 761-774"},"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}
引用次数: 0
IUBMB Trainee Initiative: supporting emerging biochemists and molecular biologists around the world 国际生物化学和分子生物学联合会受训人员计划：支持世界各地的新兴生物化学家和分子生物学家。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/j.tibs.2024.07.004
Ecaterina Cozma , Patrick Penndorf
{"title":"IUBMB Trainee Initiative: supporting emerging biochemists and molecular biologists around the world","authors":"Ecaterina Cozma ,&nbsp;Patrick Penndorf","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":"49 9","pages":"Pages 749-751"},"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}
引用次数: 0
Beyond the bench: motivations and aspirations of the IUBMB Trainee Initiative Leadership Committee 工作台之外：国际生物化学和分子生物学联合会受训人员倡议领导委员会的动机和愿望。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/j.tibs.2024.07.003
Mihaela Jovanović , Jessie Wong Ling Ai , Aishatu Muhammad Malami , Ecaterina Cozma
{"title":"Beyond the bench: motivations and aspirations of the IUBMB Trainee Initiative Leadership Committee","authors":"Mihaela Jovanović ,&nbsp;Jessie Wong Ling Ai ,&nbsp;Aishatu Muhammad Malami ,&nbsp;Ecaterina Cozma","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":"49 9","pages":"Pages 745-748"},"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}
引用次数: 0
Structural transitions modulate the chaperone activities of Grp94 结构转变调节了 Grp94 的伴侣活性。
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/j.tibs.2024.06.007
{"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":"49 9","pages":"Pages 752-753"},"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}
引用次数: 0
Subscription and Copyright Information 订阅和版权信息
IF 11.6 1区 生物学
Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI: 10.1016/S0968-0004(24)00200-7
{"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":"49 9","pages":"Page e1"},"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}
引用次数: 0
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