期刊
JOURNAL OF CELL BIOLOGY
卷 190, 期 4, 页码 623-635出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201004129
关键词
-
类别
资金
- National Institutes of Health (NIH) [GM078024]
- Burroughs Welcome Foundation
- Henry and Camille Dreyfus foundation
- Arnold and Mabel Beckman foundation
- David and Lucile Packard foundation
- NIH/National Research Service [5T32GM07616]
- Moore Foundation
- Caltech's Beckman Institute
The signal recognition particle (SRP) and SRP receptor comprise the major cellular machinery that mediates the cotranslational targeting of proteins to cellular membranes. It remains unclear how the delivery of cargos to the target membrane is spatially coordinated. We show here that phospholipid binding drives important conformational rearrangements that activate the bacterial SRP receptor FtsY and the SRP-FtsY complex. This leads to accelerated SRP-FtsY complex assembly, and allows the SRP-FtsY complex to more efficiently unload cargo proteins. Likewise, formation of an active SRP-FtsY GTPase complex exposes FtsY's lipid-binding helix and enables stable membrane association of the targeting complex. Thus, membrane binding, complex assembly with SRP, and cargo unloading are inextricably linked to each other via conformational changes in FtsY. These allosteric communications allow the membrane delivery of cargo proteins to be efficiently coupled to their subsequent unloading and translocation, thus providing spatial coordination during protein targeting.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据