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The cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers 蓝藻蛋白 VIPP1 在脂质双分子层上形成类似 ESCRT-III 的结构
Nature structural & molecular biology Pub Date : 2024-07-26 DOI: 10.1038/s41594-024-01367-7
Sichen Pan, Karin Gries, Benjamin D. Engel, Michael Schroda, Christoph A. Haselwandter, Simon Scheuring
{"title":"The cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers","authors":"Sichen Pan, Karin Gries, Benjamin D. Engel, Michael Schroda, Christoph A. Haselwandter, Simon Scheuring","doi":"10.1038/s41594-024-01367-7","DOIUrl":"https://doi.org/10.1038/s41594-024-01367-7","url":null,"abstract":"<p>The biogenesis and maintenance of thylakoid membranes require vesicle-inducing protein in plastids 1 (VIPP1). VIPP1 is a member of the endosomal sorting complex required for transport-III (ESCRT-III) superfamily, whose members form diverse filament-based supramolecular structures that facilitate membrane deformation and fission. VIPP1 cryo-electron microscopy (EM) structures in solution revealed helical rods and baskets of stacked rings, with amphipathic membrane-binding domains in the lumen. However, how VIPP1 interacts with membranes remains largely unknown. Here, using high-speed atomic force microscopy (HS-AFM), we show that VIPP1 assembles into right-handed chiral spirals and regular polygons on supported lipid bilayers via ESCRT-III-like filament assembly and dynamics. VIPP1 filaments grow clockwise into spirals through polymerization at a ring-shaped central polymerization hub, and into polygons through clockwise polymerization at the sector peripheries. Interestingly, VIPP1 initially forms Archimedean spirals, which upon maturation transform into logarithmic spirals through lateral annealing of strands to the outermore low-curvature spiral turns.</p>","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"12 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141764278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Epitranscriptome regulation. 上皮转录组调控。
Nature structural & molecular biology Pub Date : 2018-09-28 DOI: 10.1038/s41594-018-0140-7
Dan Dominissini, Gideon Rechavi
{"title":"Epitranscriptome regulation.","authors":"Dan Dominissini, Gideon Rechavi","doi":"10.1038/s41594-018-0140-7","DOIUrl":"10.1038/s41594-018-0140-7","url":null,"abstract":"","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36535441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation. 调控片段的亚基间捕获是CaMKII协同激活的一个组成部分。
Nature structural & molecular biology Pub Date : 2010-03-01 DOI: 10.1038/nsmb.1751
Luke H Chao, Patricia Pellicena, Sebastian Deindl, Lauren A Barclay, Howard Schulman, John Kuriyan
{"title":"Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation.","authors":"Luke H Chao,&nbsp;Patricia Pellicena,&nbsp;Sebastian Deindl,&nbsp;Lauren A Barclay,&nbsp;Howard Schulman,&nbsp;John Kuriyan","doi":"10.1038/nsmb.1751","DOIUrl":"https://doi.org/10.1038/nsmb.1751","url":null,"abstract":"<p><p>The dodecameric holoenzyme of calcium-calmodulin-dependent protein kinase II (CaMKII) responds to high-frequency Ca(2+) pulses to become Ca(2+) independent. A simple coincidence-detector model for Ca(2+)-frequency dependency assumes noncooperative activation of kinase domains. We show that activation of CaMKII by Ca(2+)-calmodulin is cooperative, with a Hill coefficient of approximately 3.0, implying sequential kinase-domain activation beyond dimeric units. We present data for a model in which cooperative activation includes the intersubunit 'capture' of regulatory segments. Such a capture interaction is seen in a crystal structure that shows extensive contacts between the regulatory segment of one kinase and the catalytic domain of another. These interactions are mimicked by a natural inhibitor of CaMKII. Our results show that a simple coincidence-detection model cannot be operative and point to the importance of kinetic dissection of the frequency-response mechanism in future experiments.</p>","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"17 3","pages":"264-72"},"PeriodicalIF":0.0,"publicationDate":"2010-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/nsmb.1751","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9338579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 115
Domain structure of separase and its binding to securin as determined by EM. 分离酶的结构域结构及其与securin的结合。
Nature structural & molecular biology Pub Date : 2005-06-01 Epub Date: 2005-05-08 DOI: 10.1038/nsmb935
Hector Viadiu, Olaf Stemmann, Marc W Kirschner, Thomas Walz
{"title":"Domain structure of separase and its binding to securin as determined by EM.","authors":"Hector Viadiu,&nbsp;Olaf Stemmann,&nbsp;Marc W Kirschner,&nbsp;Thomas Walz","doi":"10.1038/nsmb935","DOIUrl":"https://doi.org/10.1038/nsmb935","url":null,"abstract":"<p><p>After the degradation of its inhibitor securin, separase initiates chromosome segregation during the metaphase-to-anaphase transition by cleaving cohesin. Here we present a density map at a resolution of 25 A of negatively stained separase-securin complex. Based on labeling data and sequence analysis, we propose a model for the structure of separase, consisting of 26 ARM repeats, an unstructured region of 280 residues and two caspase-like domains, with securin binding to the ARM repeats.</p>","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"12 6","pages":"552-3"},"PeriodicalIF":0.0,"publicationDate":"2005-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1038/nsmb935","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25271368","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 51
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