Nature Reviews Molecular Cell Biology最新文献_第8页

Grand roles for microproteins 微蛋白的巨大作用

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-11-14 DOI: 10.1038/s41580-024-00806-z

Valerie A. Tornini

引用次数: 0

The intraflagellar transport cycle 叶栅内运输循环

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-11-13 DOI: 10.1038/s41580-024-00797-x

Samuel E. Lacey, Gaia Pigino

{"title":"The intraflagellar transport cycle","authors":"Samuel E. Lacey, Gaia Pigino","doi":"10.1038/s41580-024-00797-x","DOIUrl":"10.1038/s41580-024-00797-x","url":null,"abstract":"Primary and motile cilia are eukaryotic organelles that perform crucial roles in cellular signalling and motility. Intraflagellar transport (IFT) contributes to the formation of the highly specialized ciliary proteome by active and selective transport of soluble and membrane proteins into and out of cilia. IFT is performed by the IFT-A and IFT-B protein complexes, which together link cargoes to the microtubule motors kinesin and dynein. In this Review, we discuss recent structural and mechanistic insights on how the IFT complexes are first recruited to the base of the cilium, how they polymerize into an anterograde IFT train, and how this complex imports cargoes from the cytoplasm. We will describe insights into how kinesin-driven anterograde trains are carried to the ciliary tip, where they are remodelled into dynein-driven retrograde trains for cargo export. We will also present how the interplay between IFT-A and IFT-B complexes, motor proteins and cargo adaptors is regulated for bidirectional ciliary transport. Intraflagellar transport (IFT) ensures delivery of selected proteins into cilia. The IFT protein complexes IFT-A and IFT-B polymerize at the base of the cilium to form an anterograde train that facilitates cargo import, whereas remodelling into a retrograde train at the ciliary tip enables cargo export.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"26 3","pages":"175-192"},"PeriodicalIF":81.3,"publicationDate":"2024-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142609901","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

Author Correction: All the sites we cannot see: Sources and mitigation of false negatives in RNA modification studies 作者更正：所有我们看不见的地方RNA 修饰研究中假阴性的来源与缓解

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-11-12 DOI: 10.1038/s41580-024-00810-3

Shalini Oberdoerffer, Wendy V. Gilbert

引用次数: 0

Transcription regulation by biomolecular condensates 生物分子凝聚体的转录调控

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-11-08 DOI: 10.1038/s41580-024-00789-x

Gaofeng Pei, Heankel Lyons, Pilong Li, Benjamin R. Sabari

{"title":"Transcription regulation by biomolecular condensates","authors":"Gaofeng Pei, Heankel Lyons, Pilong Li, Benjamin R. Sabari","doi":"10.1038/s41580-024-00789-x","DOIUrl":"10.1038/s41580-024-00789-x","url":null,"abstract":"Biomolecular condensates regulate transcription by dynamically compartmentalizing the transcription machinery. Classic models of transcription regulation focus on the recruitment and regulation of RNA polymerase II by the formation of complexes at the 1–10 nm length scale, which are driven by structured and stoichiometric interactions. These complexes are further organized into condensates at the 100–1,000 nm length scale, which are driven by dynamic multivalent interactions often involving domain–ligand pairs or intrinsically disordered regions. Regulation through condensate-mediated organization does not supersede the processes occurring at the 1–10 nm scale, but it provides regulatory mechanisms for promoting or preventing these processes in the crowded nuclear environment. Regulation of transcription by transcriptional condensates is involved in cell state transitions during animal and plant development, cell signalling and cellular responses to the environment. These condensate-mediated processes are dysregulated in developmental disorders, cancer and neurodegeneration. In this Review, we discuss the principles underlying the regulation of transcriptional condensates, their roles in physiology and their dysregulation in human diseases. Transcriptional condensates, which are formed through dynamic multivalent interactions between proteins, RNA and chromatin, regulate transcription by compartmentalizing its machinery in the crowded nuclear environment. These condensates regulate animal and plant development, cell signalling and responses to the environment, and they are dysregulated in developmental disorders, cancer and neurodegeneration.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"26 3","pages":"213-236"},"PeriodicalIF":81.3,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142596850","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

Homeostasis control in health and disease by the unfolded protein response 未折叠蛋白反应对健康和疾病的平衡控制

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-11-05 DOI: 10.1038/s41580-024-00794-0

Diego Acosta-Alvear, Jonathan M. Harnoss, Peter Walter, Avi Ashkenazi

{"title":"Homeostasis control in health and disease by the unfolded protein response","authors":"Diego Acosta-Alvear, Jonathan M. Harnoss, Peter Walter, Avi Ashkenazi","doi":"10.1038/s41580-024-00794-0","DOIUrl":"10.1038/s41580-024-00794-0","url":null,"abstract":"Cells rely on the endoplasmic reticulum (ER) to fold and assemble newly synthesized transmembrane and secretory proteins — essential for cellular structure–function and for both intracellular and intercellular communication. To ensure the operative fidelity of the ER, eukaryotic cells leverage the unfolded protein response (UPR) — a stress-sensing and signalling network that maintains homeostasis by rebalancing the biosynthetic capacity of the ER according to need. The metazoan UPR can also redirect signalling from cytoprotective adaptation to programmed cell death if homeostasis restoration fails. As such, the UPR benefits multicellular organisms by preserving optimally functioning cells while removing damaged ones. Nevertheless, dysregulation of the UPR can be harmful. In this Review, we discuss the UPR and its regulatory processes as a paradigm in health and disease. We highlight important recent advances in molecular and mechanistic understanding of the UPR that enable greater precision in designing and developing innovative strategies to harness its potential for therapeutic gain. We underscore the rheostatic character of the UPR, its contextual nature and critical open questions for its further elucidation. The unfolded protein response is a stress-sensing and signalling network that maintains homeostasis by regulating the biosynthetic capacity of the endoplasmic reticulum and induces cell death when homeostasis is not restored. This Review discusses the mechanisms of action of the UPR, its interactions with other cellular processes, roles in disease and possible therapeutic interventions.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"26 3","pages":"193-212"},"PeriodicalIF":81.3,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142580710","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

Epigenetic discovery by enzyme activity profiling 通过酶活性分析发现表观遗传学

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-10-25 DOI: 10.1038/s41580-024-00801-4

Manini S. Penikalapati, Jordan L. Meier

引用次数: 0

The double-edged sword of eliminating senescent cells 消除衰老细胞的双刃剑

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-10-24 DOI: 10.1038/s41580-024-00798-w

Eric Gilson

引用次数: 0

When senescence generates pluripotent stem cells 当衰老产生多能干细胞时

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-10-24 DOI: 10.1038/s41580-024-00799-9

Miria Ricchetti

引用次数: 0

A nuclear morphology-based machine learning algorithm for senescence detection 基于核形态学的衰老检测机器学习算法

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-10-23 DOI: 10.1038/s41580-024-00796-y

Imanol Duran

引用次数: 0

The prompt to discover senolytics 发现老年痴呆症的提示

IF 81.3 1区生物学

Nature Reviews Molecular Cell Biology Pub Date : 2024-10-23 DOI: 10.1038/s41580-024-00795-z

James L. Kirkland

引用次数: 0