Pub Date : 2025-11-05DOI: 10.1038/s41580-025-00929-x
Lisa Heinke
A study finds that mechanical activation leads to microtubule rearrangement, facilitating the proteasomal degradation of an inhibitor of YAP/TAZ, thus promoting YAP/TAZ nuclear translocation.
{"title":"Microtubules provide a mechanical link for YAP/TAZ signalling","authors":"Lisa Heinke","doi":"10.1038/s41580-025-00929-x","DOIUrl":"10.1038/s41580-025-00929-x","url":null,"abstract":"A study finds that mechanical activation leads to microtubule rearrangement, facilitating the proteasomal degradation of an inhibitor of YAP/TAZ, thus promoting YAP/TAZ nuclear translocation.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"26 12","pages":"903-903"},"PeriodicalIF":90.2,"publicationDate":"2025-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145440939","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}
Pub Date : 2025-11-05DOI: 10.1038/s41580-025-00926-0
Crisanto Gutierrez
{"title":"Discovery of a human gene encoding a cyclin-dependent kinase","authors":"Crisanto Gutierrez","doi":"10.1038/s41580-025-00926-0","DOIUrl":"https://doi.org/10.1038/s41580-025-00926-0","url":null,"abstract":"","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"38 1","pages":""},"PeriodicalIF":112.7,"publicationDate":"2025-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145440936","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}
Pub Date : 2025-11-03DOI: 10.1038/s41580-025-00920-6
Fabricio Loayza-Puch
The discovery of noncanonical short open reading frames that produce functional microproteins upended our perception of large parts of our genome as ‘noncoding’.
产生功能性微蛋白的非规范短开放阅读框的发现颠覆了我们对大部分基因组为“非编码”的看法。
{"title":"Revealing the hidden coding potential of the human genome","authors":"Fabricio Loayza-Puch","doi":"10.1038/s41580-025-00920-6","DOIUrl":"10.1038/s41580-025-00920-6","url":null,"abstract":"The discovery of noncanonical short open reading frames that produce functional microproteins upended our perception of large parts of our genome as ‘noncoding’.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"27 2","pages":"93-93"},"PeriodicalIF":90.2,"publicationDate":"2025-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145427582","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}
Pub Date : 2025-11-03DOI: 10.1038/s41580-025-00925-1
Christian Kofoed
In this Tools of the Trade article, Kofoed (Muir lab) describes the development of the dual-component platform splicing-modulated actuation upon recognition of targets (SMART), which combines detection of cells with specific surface markers with a customizable output.
{"title":"Transforming cell-surface signatures into customizable protein functions","authors":"Christian Kofoed","doi":"10.1038/s41580-025-00925-1","DOIUrl":"10.1038/s41580-025-00925-1","url":null,"abstract":"In this Tools of the Trade article, Kofoed (Muir lab) describes the development of the dual-component platform splicing-modulated actuation upon recognition of targets (SMART), which combines detection of cells with specific surface markers with a customizable output.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"27 2","pages":"91-91"},"PeriodicalIF":90.2,"publicationDate":"2025-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145427580","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}
Pub Date : 2025-11-03DOI: 10.1038/s41580-025-00924-2
Siyuan Wang
Siyuan (Steven) Wang discusses a 1984 study that reported that transcriptional regulation (in this case, in bacteria) depends on the formation of DNA loops.
{"title":"DNA looping regulates transcription","authors":"Siyuan Wang","doi":"10.1038/s41580-025-00924-2","DOIUrl":"10.1038/s41580-025-00924-2","url":null,"abstract":"Siyuan (Steven) Wang discusses a 1984 study that reported that transcriptional regulation (in this case, in bacteria) depends on the formation of DNA loops.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"27 2","pages":"94-94"},"PeriodicalIF":90.2,"publicationDate":"2025-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145427583","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}
Pub Date : 2025-11-03DOI: 10.1038/s41580-025-00923-3
Drishan Dahal
In this Tools of the Trade article, Dahal (Rehling lab) discusses the development of a polymorpholino oligonucleotide chimera tool that enables selective and efficient silencing of mitochondrial mRNA.
{"title":"Silencing of mitochondrial gene expression using polymorpholino chimeras","authors":"Drishan Dahal","doi":"10.1038/s41580-025-00923-3","DOIUrl":"10.1038/s41580-025-00923-3","url":null,"abstract":"In this Tools of the Trade article, Dahal (Rehling lab) discusses the development of a polymorpholino oligonucleotide chimera tool that enables selective and efficient silencing of mitochondrial mRNA.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"27 1","pages":"8-8"},"PeriodicalIF":90.2,"publicationDate":"2025-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145427581","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}
Pub Date : 2025-10-31DOI: 10.1038/s41580-025-00919-z
Leo Kiss
In this Tools of the Trade article, Kiss (Schulman lab) discusses the development of UbiREAD, a method that delivers in vitro-ubiquitinated protein reporters into cells to systematically assess how different ubiquitin chain configurations affect protein stability and degradation.
{"title":"Decoding ubiquitin signals inside cells","authors":"Leo Kiss","doi":"10.1038/s41580-025-00919-z","DOIUrl":"10.1038/s41580-025-00919-z","url":null,"abstract":"In this Tools of the Trade article, Kiss (Schulman lab) discusses the development of UbiREAD, a method that delivers in vitro-ubiquitinated protein reporters into cells to systematically assess how different ubiquitin chain configurations affect protein stability and degradation.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"26 12","pages":"905-905"},"PeriodicalIF":90.2,"publicationDate":"2025-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145411768","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}
Pub Date : 2025-10-27DOI: 10.1038/s41580-025-00890-9
Anne Wentink, Rina Rosenzweig, Harm Kampinga, Bernd Bukau
The 70-kDa heat shock protein (Hsp70) chaperone is essential to maintain cellular protein homeostasis, facilitating the folding, assembly, membrane translocation and quality control of proteins. Hsp70s achieve their functions through ‘selective promiscuity’, interacting with a wide range of substrate proteins while minimizing undesired interactions. J-domain proteins (JDPs) and nucleotide exchange factors (NEFs) are key to substrate recognition, remodelling and release from chaperone complexes. JDPs either target Hsp70s to specific subcellular sites where substrates reside (recruiters) or bind substrates directly by using highly specific (specialists) or multiple, versatile (generalists) binding sites. Through diverse substrate-binding modes and regulatory mechanisms, the 50 human JDPs confer remarkable client specificity to Hsp70s, a function that is comparable to that achieved by close to 600 E3 ubiquitin ligases in targeting proteins for degradation. Moreover, JDPs, together with NEFs, dictate the fate of Hsp70 clients by directing them to distinct protein quality control pathways, resulting in their folding or degradation. These recent mechanistic insights into Hsp70 regulation not only highlight the versatility and complexity of the Hsp70 network but also offer new avenues for more specific interventions in ageing-related and other protein folding diseases. Hsp70 chaperones facilitate protein folding, complex assembly and translocation through membranes. This Review discusses recent insights into how Hsp70 and its co-chaperones — J-domain proteins and nucleotide exchange factors — exert such functions, achieve substrate specificity and determine protein fate (folding or degradation).
{"title":"Mechanisms and regulation of the Hsp70 chaperone network","authors":"Anne Wentink, Rina Rosenzweig, Harm Kampinga, Bernd Bukau","doi":"10.1038/s41580-025-00890-9","DOIUrl":"10.1038/s41580-025-00890-9","url":null,"abstract":"The 70-kDa heat shock protein (Hsp70) chaperone is essential to maintain cellular protein homeostasis, facilitating the folding, assembly, membrane translocation and quality control of proteins. Hsp70s achieve their functions through ‘selective promiscuity’, interacting with a wide range of substrate proteins while minimizing undesired interactions. J-domain proteins (JDPs) and nucleotide exchange factors (NEFs) are key to substrate recognition, remodelling and release from chaperone complexes. JDPs either target Hsp70s to specific subcellular sites where substrates reside (recruiters) or bind substrates directly by using highly specific (specialists) or multiple, versatile (generalists) binding sites. Through diverse substrate-binding modes and regulatory mechanisms, the 50 human JDPs confer remarkable client specificity to Hsp70s, a function that is comparable to that achieved by close to 600 E3 ubiquitin ligases in targeting proteins for degradation. Moreover, JDPs, together with NEFs, dictate the fate of Hsp70 clients by directing them to distinct protein quality control pathways, resulting in their folding or degradation. These recent mechanistic insights into Hsp70 regulation not only highlight the versatility and complexity of the Hsp70 network but also offer new avenues for more specific interventions in ageing-related and other protein folding diseases. Hsp70 chaperones facilitate protein folding, complex assembly and translocation through membranes. This Review discusses recent insights into how Hsp70 and its co-chaperones — J-domain proteins and nucleotide exchange factors — exert such functions, achieve substrate specificity and determine protein fate (folding or degradation).","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"27 2","pages":"110-128"},"PeriodicalIF":90.2,"publicationDate":"2025-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145373842","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}
Pub Date : 2025-10-17DOI: 10.1038/s41580-025-00908-2
Ellen Kazumi Okuda, Laurell Fridolin Kessler
In this Tools of the Trade article, Okuda and Kessler (Müller-McNicoll and Heilemann labs) discuss how the combination of two novel methods enabled them to study the architecture and interaction of nuclear membraneless organelles.
{"title":"A new rapid-degradation system combined with super-resolution microscopy","authors":"Ellen Kazumi Okuda, Laurell Fridolin Kessler","doi":"10.1038/s41580-025-00908-2","DOIUrl":"10.1038/s41580-025-00908-2","url":null,"abstract":"In this Tools of the Trade article, Okuda and Kessler (Müller-McNicoll and Heilemann labs) discuss how the combination of two novel methods enabled them to study the architecture and interaction of nuclear membraneless organelles.","PeriodicalId":19051,"journal":{"name":"Nature Reviews Molecular Cell Biology","volume":"26 12","pages":"904-904"},"PeriodicalIF":90.2,"publicationDate":"2025-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145311249","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}
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