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TitleA recombinant BBSome core complex and how it interacts with ciliary cargo.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateNov 15, 2017
AuthorsBjörn Udo Klink / Eldar Zent / Puneet Juneja / Anne Kuhlee / Stefan Raunser / Alfred Wittinghofer /
PubMed AbstractCilia are small, antenna-like structures on the surface of eukaryotic cells that harbor a unique set of sensory proteins, including GPCRs and other membrane proteins. The transport of these proteins ...Cilia are small, antenna-like structures on the surface of eukaryotic cells that harbor a unique set of sensory proteins, including GPCRs and other membrane proteins. The transport of these proteins involves the BBSome, an eight-membered protein complex that is recruited to ciliary membranes by the G-protein Arl6. BBSome malfunction leads to Bardet-Biedl syndrome, a ciliopathy with severe consequences. Short ciliary targeting sequences (CTS) have been identified that trigger the transport of ciliary proteins. However, mechanistic studies that relate ciliary targeting to BBSome binding are missing. Here we used heterologously expressed BBSome subcomplexes to analyze the complex architecture and to investigate the binding of GPCRs and other receptors to the BBSome. A stable heterohexameric complex was identified that binds to GPCRs with interactions that only partially overlap with previously described CTS, indicating a more complex recognition than anticipated. Arl6•GTP does not affect these interactions, suggesting no direct involvement in cargo loading/unloading.
External linksElife / PubMed:29168691 / PubMed Central
MethodsEM (single particle)
Resolution23.0 Å
Structure data

EMDB-3712:
Human BBsome core complex with subunits BBS1, BBS4, BBS5, BBS8, BBS9, BBS18
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Homo sapiens (human)

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