期刊
STRUCTURE
卷 27, 期 9, 页码 1384-+出版社
CELL PRESS
DOI: 10.1016/j.str.2019.06.006
关键词
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资金
- NIGMS [R01-GM089933, R01-GM123089, P41-GM103311]
- Austrian Science Fund [FWF P30162]
- Damon Runyon Fellowship [DRG 2160-13]
- NIGMS fellowship [F32-GM089218]
- NEI [EY002162]
- Research to Prevent Blindness Unrestricted Grant
- Howard Hughes Medical Institute
- Blavatnik Family Foundation
The unique membrane composition of cilia is maintained by a diffusion barrier at the transition zone that is breached when the BBSome escorts signaling receptors out of cilia. Understanding how the BBSome removes proteins from cilia has been hampered by a lack of structural information. Here, we present a nearly complete C alpha model of BBSome purified from cow retina. The model is based on a single-particle cryo-electron microscopy density map at 4.9-angstrom resolution that was interpreted with the help of comprehensive Rosetta-based structural modeling constrained by crosslinking mass spectrometry data. We find that BBSome subunits have a very high degree of interconnectivity, explaining the obligate nature of the complex. Furthermore, like other coat adaptors, the BBSome exists in an autoinhibited state in solution and must thus undergo a conformational change upon recruitment to membranes by the small GTPase ARL6/BBS3. Our model provides the first detailed view of the machinery enabling ciliary exit.
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