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TitleNear-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJun 8, 2020
AuthorsShuang Yang / Kriti Bahl / Hui-Ting Chou / Jonathan Woodsmith / Ulrich Stelzl / Thomas Walz / Maxence V Nachury /
PubMed AbstractDynamic trafficking of G protein-coupled receptors (GPCRs) out of cilia is mediated by the BBSome. In concert with its membrane recruitment factor, the small GTPase ARL6/BBS3, the BBSome ferries ...Dynamic trafficking of G protein-coupled receptors (GPCRs) out of cilia is mediated by the BBSome. In concert with its membrane recruitment factor, the small GTPase ARL6/BBS3, the BBSome ferries GPCRs across the transition zone, a diffusion barrier at the base of cilia. Here, we present the near-atomic structures of the BBSome by itself and in complex with ARL6, and we describe the changes in BBSome conformation induced by ARL6 binding. Modeling the interactions of the BBSome with membranes and the GPCR Smoothened (SMO) reveals that SMO, and likely also other GPCR cargoes, must release their amphipathic helix 8 from the membrane to be recognized by the BBSome.
External linksElife / PubMed:32510327 / PubMed Central
MethodsEM (single particle)
Resolution3.44 - 4.0 Å
Structure data

21251

6vnw

EMDB-21251, PDB-6vnw:
Cryo-EM structure of apo-BBSome
Method: EM (single particle) / Resolution: 3.44 Å

21259

6voa

EMDB-21259, PDB-6voa:
Cryo-EM structure of the BBSome-ARL6 complex
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • bos taurus (cattle)
KeywordsPROTEIN TRANSPORT / Cilia / Bardet-Biedl Syndrome

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