质子如何塑造 AMPA 受体的结构、功能和在突触中的扩散

Nature structural & molecular biology Pub Date : 2024-08-13 DOI:10.1038/s41594-024-01371-x

{"title":"质子如何塑造 AMPA 受体的结构、功能和在突触中的扩散","authors":"","doi":"10.1038/s41594-024-01371-x","DOIUrl":null,"url":null,"abstract":"The extracellular AMPA receptor N-terminal domain (NTD) affects synaptic strength by tuning receptor diffusion. We reveal that pH fluctuations accompanying synaptic activity alter NTD conformation of the functionally dominant GluA2 subunit, via proton sensing by an NTD histidine residue, thereby increasing gating kinetics and receptor diffusion at the synapse.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"How protons shape AMPA receptor structure, function and diffusion at the synapse\",\"authors\":\"\",\"doi\":\"10.1038/s41594-024-01371-x\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The extracellular AMPA receptor N-terminal domain (NTD) affects synaptic strength by tuning receptor diffusion. We reveal that pH fluctuations accompanying synaptic activity alter NTD conformation of the functionally dominant GluA2 subunit, via proton sensing by an NTD histidine residue, thereby increasing gating kinetics and receptor diffusion at the synapse.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-08-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature structural & molecular biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-024-01371-x\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature structural & molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-024-01371-x","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 0

摘要

细胞外 AMPA 受体 N 端结构域（NTD）通过调整受体扩散影响突触强度。我们揭示了伴随突触活动的 pH 波动通过 NTD 组氨酸残基的质子感应改变了功能上占主导地位的 GluA2 亚基的 NTD 构象，从而增加了门控动力学和受体在突触处的扩散。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

摘要图片

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

How protons shape AMPA receptor structure, function and diffusion at the synapse

The extracellular AMPA receptor N-terminal domain (NTD) affects synaptic strength by tuning receptor diffusion. We reveal that pH fluctuations accompanying synaptic activity alter NTD conformation of the functionally dominant GluA2 subunit, via proton sensing by an NTD histidine residue, thereby increasing gating kinetics and receptor diffusion at the synapse.

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

Nature structural & molecular biology

自引率

0.00%

发文量