鞭毛内转运蛋白传递到纤毛基部并组装成序列

IF 12.5 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Aniruddha Mitra, Evangelos Gioukakis, Wouter Mul, Erwin J. G. Peterman
{"title":"鞭毛内转运蛋白传递到纤毛基部并组装成序列","authors":"Aniruddha Mitra,&nbsp;Evangelos Gioukakis,&nbsp;Wouter Mul,&nbsp;Erwin J. G. Peterman","doi":"10.1126/sciadv.adr1716","DOIUrl":null,"url":null,"abstract":"<div >Anterograde intraflagellar transport (IFT) trains, composed of IFT-B, IFT-A, and BBSome subcomplexes, are responsible for transporting ciliary proteins into the cilium. How IFT subcomplexes reach the ciliary base and assemble into IFT trains is poorly understood. Here, we perform quantitative single-molecule imaging in <i>Caenorhabditis elegans</i> chemosensory cilia to uncover how IFT subcomplexes arrive at the base, organize in IFT trains, and enter the cilium. We find that BBSomes reach the base via diffusion where they either associate with assembling IFT trains or with the membrane surrounding the base. In contrast, IFT-B and IFT-A reach the base via directed transport most likely on vesicles that stop at distinct locations near the base. Individual subcomplexes detach from the vesicles into a diffusive pool and associate to assembling trains. Our results show that IFT-B is first incorporated into IFT trains, followed by IFT-A, and finally BBSomes, indicating that the assembly of IFT trains is a highly regulated, step-wise process.</div>","PeriodicalId":21609,"journal":{"name":"Science Advances","volume":"11 14","pages":""},"PeriodicalIF":12.5000,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.science.org/doi/reader/10.1126/sciadv.adr1716","citationCount":"0","resultStr":"{\"title\":\"Delivery of intraflagellar transport proteins to the ciliary base and assembly into trains\",\"authors\":\"Aniruddha Mitra,&nbsp;Evangelos Gioukakis,&nbsp;Wouter Mul,&nbsp;Erwin J. G. Peterman\",\"doi\":\"10.1126/sciadv.adr1716\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div >Anterograde intraflagellar transport (IFT) trains, composed of IFT-B, IFT-A, and BBSome subcomplexes, are responsible for transporting ciliary proteins into the cilium. How IFT subcomplexes reach the ciliary base and assemble into IFT trains is poorly understood. Here, we perform quantitative single-molecule imaging in <i>Caenorhabditis elegans</i> chemosensory cilia to uncover how IFT subcomplexes arrive at the base, organize in IFT trains, and enter the cilium. We find that BBSomes reach the base via diffusion where they either associate with assembling IFT trains or with the membrane surrounding the base. In contrast, IFT-B and IFT-A reach the base via directed transport most likely on vesicles that stop at distinct locations near the base. Individual subcomplexes detach from the vesicles into a diffusive pool and associate to assembling trains. Our results show that IFT-B is first incorporated into IFT trains, followed by IFT-A, and finally BBSomes, indicating that the assembly of IFT trains is a highly regulated, step-wise process.</div>\",\"PeriodicalId\":21609,\"journal\":{\"name\":\"Science Advances\",\"volume\":\"11 14\",\"pages\":\"\"},\"PeriodicalIF\":12.5000,\"publicationDate\":\"2025-04-04\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.science.org/doi/reader/10.1126/sciadv.adr1716\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Science Advances\",\"FirstCategoryId\":\"103\",\"ListUrlMain\":\"https://www.science.org/doi/10.1126/sciadv.adr1716\",\"RegionNum\":1,\"RegionCategory\":\"综合性期刊\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science Advances","FirstCategoryId":"103","ListUrlMain":"https://www.science.org/doi/10.1126/sciadv.adr1716","RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
引用次数: 0

摘要

由IFT- b、IFT- a和BBSome亚复合物组成的顺行纤毛内运输(IFT)序列负责将纤毛蛋白运输到纤毛中。IFT亚复合物如何到达纤毛碱基并组装成IFT序列尚不清楚。在这里,我们对秀丽隐杆线虫的化学感觉纤毛进行了定量单分子成像,以揭示IFT亚复合物如何到达基部,在IFT序列中组织,并进入纤毛。我们发现BBSomes通过扩散到达碱基,在那里它们要么与组装IFT序列结合,要么与围绕碱基的膜结合。相比之下,IFT-B和IFT-A通过定向运输到达碱基,最有可能通过停在碱基附近不同位置的囊泡到达。单个亚复合物从囊泡中分离到扩散池中,并与组装序列相结合。我们的研究结果表明,IFT- b首先被纳入IFT序列,然后是IFT- a,最后是BBSomes,这表明IFT序列的组装是一个高度调控的、逐步的过程。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Delivery of intraflagellar transport proteins to the ciliary base and assembly into trains

Delivery of intraflagellar transport proteins to the ciliary base and assembly into trains
Anterograde intraflagellar transport (IFT) trains, composed of IFT-B, IFT-A, and BBSome subcomplexes, are responsible for transporting ciliary proteins into the cilium. How IFT subcomplexes reach the ciliary base and assemble into IFT trains is poorly understood. Here, we perform quantitative single-molecule imaging in Caenorhabditis elegans chemosensory cilia to uncover how IFT subcomplexes arrive at the base, organize in IFT trains, and enter the cilium. We find that BBSomes reach the base via diffusion where they either associate with assembling IFT trains or with the membrane surrounding the base. In contrast, IFT-B and IFT-A reach the base via directed transport most likely on vesicles that stop at distinct locations near the base. Individual subcomplexes detach from the vesicles into a diffusive pool and associate to assembling trains. Our results show that IFT-B is first incorporated into IFT trains, followed by IFT-A, and finally BBSomes, indicating that the assembly of IFT trains is a highly regulated, step-wise process.
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
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信