动力蛋白I磷酸化与突触囊泡内吞的控制。

Biochemical Society Symposia Pub Date : 2005-01-01 DOI:10.1042/bss0720087

Karen J Smillie, Michael A Cousin

{"title":"动力蛋白I磷酸化与突触囊泡内吞的控制。","authors":"Karen J Smillie, Michael A Cousin","doi":"10.1042/bss0720087","DOIUrl":null,"url":null,"abstract":"The GTPase dynamin I is essential for synaptic vesicle endocytosis in nerve terminals. It is a nerve terminal phosphoprotein that is dephosphorylated on nerve terminal stimulation by the calcium-dependent protein phosphatase calcineurin and then rephosphorylated by cyclin-dependent kinase 5 on termination of the stimulus. Because of its unusual phosphorylation profile, the phosphorylation status of dynamin I was assumed to be inexorably linked to synaptic vesicle endocytosis; however, direct proof of this link has been elusive until very recently. This review will describe current knowledge regarding dynamin I phosphorylation in nerve terminals and how this regulates its biological function with respect to synaptic vesicle endocytosis.","PeriodicalId":55383,"journal":{"name":"Biochemical Society Symposia","volume":" 72","pages":"87-97"},"PeriodicalIF":0.0000,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2077358/pdf/nihms-1150.pdf","citationCount":"51","resultStr":"{\"title\":\"Dynamin I phosphorylation and the control of synaptic vesicle endocytosis.\",\"authors\":\"Karen J Smillie, Michael A Cousin\",\"doi\":\"10.1042/bss0720087\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The GTPase dynamin I is essential for synaptic vesicle endocytosis in nerve terminals. It is a nerve terminal phosphoprotein that is dephosphorylated on nerve terminal stimulation by the calcium-dependent protein phosphatase calcineurin and then rephosphorylated by cyclin-dependent kinase 5 on termination of the stimulus. Because of its unusual phosphorylation profile, the phosphorylation status of dynamin I was assumed to be inexorably linked to synaptic vesicle endocytosis; however, direct proof of this link has been elusive until very recently. This review will describe current knowledge regarding dynamin I phosphorylation in nerve terminals and how this regulates its biological function with respect to synaptic vesicle endocytosis.\",\"PeriodicalId\":55383,\"journal\":{\"name\":\"Biochemical Society Symposia\",\"volume\":\" 72\",\"pages\":\"87-97\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2005-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2077358/pdf/nihms-1150.pdf\",\"citationCount\":\"51\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemical Society Symposia\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1042/bss0720087\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical Society Symposia","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1042/bss0720087","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 51

摘要

GTPase动力蛋白I对神经末梢突触囊泡内吞作用至关重要。它是一种神经末梢磷酸化蛋白，在钙依赖性蛋白磷酸酶钙调磷酸酶的神经末梢刺激下被去磷酸化，然后在刺激终止时被细胞周期蛋白依赖性激酶5再磷酸化。由于其不寻常的磷酸化特征，动力蛋白1的磷酸化状态被认为与突触囊泡内吞作用有着不可避免的联系;然而，这种联系的直接证据一直难以捉摸，直到最近。这篇综述将描述目前关于神经末梢动力蛋白I磷酸化的知识，以及它如何调节其在突触囊泡内吞作用方面的生物学功能。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

Dynamin I phosphorylation and the control of synaptic vesicle endocytosis.

The GTPase dynamin I is essential for synaptic vesicle endocytosis in nerve terminals. It is a nerve terminal phosphoprotein that is dephosphorylated on nerve terminal stimulation by the calcium-dependent protein phosphatase calcineurin and then rephosphorylated by cyclin-dependent kinase 5 on termination of the stimulus. Because of its unusual phosphorylation profile, the phosphorylation status of dynamin I was assumed to be inexorably linked to synaptic vesicle endocytosis; however, direct proof of this link has been elusive until very recently. This review will describe current knowledge regarding dynamin I phosphorylation in nerve terminals and how this regulates its biological function with respect to synaptic vesicle endocytosis.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Biochemical Society Symposia

自引率

0.00%

发文量

期刊最新文献

Pleckstrin homology (PH) domains and phosphoinositides. Evolutionarily conserved structural and functional roles of the FYVE domain. The role of the phosphoinositides at the Golgi complex. PtdIns5P: a little phosphoinositide with big functions? Our FABulous VACation: a decade of phosphatidylinositol 3,5-bisphosphate.