Clathrin 通过收缩膜孔介导膜裂变和出芽。

IF 13 1区 生物学 Q1 CELL BIOLOGY Cell Discovery Pub Date : 2024-06-11 DOI:10.1038/s41421-024-00677-w
Lisi Wei, Xiaoli Guo, Ehud Haimov, Kazuki Obashi, Sung Hoon Lee, Wonchul Shin, Min Sun, Chung Yu Chan, Jiansong Sheng, Zhen Zhang, Ammar Mohseni, Sudhriti Ghosh Dastidar, Xin-Sheng Wu, Xin Wang, Sue Han, Gianvito Arpino, Bo Shi, Maryam Molakarimi, Jessica Matthias, Christian A Wurm, Lin Gan, Justin W Taraska, Michael M Kozlov, Ling-Gang Wu
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引用次数: 0

摘要

膜萌发是内吞、细胞内贩运和病毒感染等基本过程的基础,一般认为膜衣形成蛋白(包括观察到最多的凝集蛋白)参与膜萌发以形成Ω形轮廓,而螺旋形成蛋白(如达能蛋白)则收缩Ω形轮廓的孔,从而介导裂变。我们对这一基本概念提出了质疑,并报告说Ω-profiles孔的关闭需要聚合的凝集蛋白,而且在神经内分泌嗜铬细胞中,Ω-profiles基底/孔区域周围的凝集蛋白介导孔的收缩/关闭。数学模型表明,Ω-profiles基底/孔区的凝集素聚合产生的力来自其固有的弯曲形状,从而使孔道收缩/关闭。这种新的裂变功能可能比凝集素在凝集素(外皮)依赖性内吞过程中众所周知的外皮形成功能产生更广泛的影响,因为它不仅是凝集素(外皮)依赖性内吞的基础,也是多种内吞模式的基础,包括超快、快速、慢速、大体积和超调内吞,以前在绒毛膜细胞中被认为是凝集素(外皮)依赖性内吞。它介导了以前被认为真正不依赖于凝集素的 "接吻-奔跑 "融合(融合孔关闭),并限制了囊泡内容物的释放速度。此外,与在绒毛膜细胞中的结果类似,我们发现在海马突触的快速和慢速内吞过程中,凝集素是必不可少的,而以前认为凝集素是可有可无的。这些结果表明,凝集素和其他可能的内在弯曲衣壳蛋白是一类新的裂变蛋白,是囊泡出芽和融合的基础。半个世纪以来,将囊泡包被内容物的功能归因于Ω轮廓的形成,并将出芽分为包被蛋白(如凝集蛋白)依赖型或不依赖型的概念和研究可能需要重新定义,并通过考虑凝集蛋白在孔收缩/关闭中的关键作用来重新审视。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Clathrin mediates membrane fission and budding by constricting membrane pores.

Membrane budding, which underlies fundamental processes like endocytosis, intracellular trafficking, and viral infection, is thought to involve membrane coat-forming proteins, including the most observed clathrin, to form Ω-shape profiles and helix-forming proteins like dynamin to constrict Ω-profiles' pores and thus mediate fission. Challenging this fundamental concept, we report that polymerized clathrin is required for Ω-profiles' pore closure and that clathrin around Ω-profiles' base/pore region mediates pore constriction/closure in neuroendocrine chromaffin cells. Mathematical modeling suggests that clathrin polymerization at Ω-profiles' base/pore region generates forces from its intrinsically curved shape to constrict/close the pore. This new fission function may exert broader impacts than clathrin's well-known coat-forming function during clathrin (coat)-dependent endocytosis, because it underlies not only clathrin (coat)-dependent endocytosis, but also diverse endocytic modes, including ultrafast, fast, slow, bulk, and overshoot endocytosis previously considered clathrin (coat)-independent in chromaffin cells. It mediates kiss-and-run fusion (fusion pore closure) previously considered bona fide clathrin-independent, and limits the vesicular content release rate. Furthermore, analogous to results in chromaffin cells, we found that clathrin is essential for fast and slow endocytosis at hippocampal synapses where clathrin was previously considered dispensable, suggesting clathrin in mediating synaptic vesicle endocytosis and fission. These results suggest that clathrin and likely other intrinsically curved coat proteins are a new class of fission proteins underlying vesicle budding and fusion. The half-a-century concept and studies that attribute vesicle-coat contents' function to Ω-profile formation and classify budding as coat-protein (e.g., clathrin)-dependent or -independent may need to be re-defined and re-examined by considering clathrin's pivotal role in pore constriction/closure.

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来源期刊
Cell Discovery
Cell Discovery Biochemistry, Genetics and Molecular Biology-Molecular Biology
CiteScore
24.20
自引率
0.60%
发文量
120
审稿时长
20 weeks
期刊介绍: Cell Discovery is a cutting-edge, open access journal published by Springer Nature in collaboration with the Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences (CAS). Our aim is to provide a dynamic and accessible platform for scientists to showcase their exceptional original research. Cell Discovery covers a wide range of topics within the fields of molecular and cell biology. We eagerly publish results of great significance and that are of broad interest to the scientific community. With an international authorship and a focus on basic life sciences, our journal is a valued member of Springer Nature's prestigious Molecular Cell Biology journals. In summary, Cell Discovery offers a fresh approach to scholarly publishing, enabling scientists from around the world to share their exceptional findings in molecular and cell biology.
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