Near-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes.
Ontology highlight
ABSTRACT:
SUBMITTER: Yang S
PROVIDER: S-EPMC7311171 | biostudies-literature | 2020 Jun
REPOSITORIES: biostudies-literature
Publications
Near-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes.
Yang Shuang S Bahl Kriti K Chou Hui-Ting HT Woodsmith Jonathan J Stelzl Ulrich U Walz Thomas T Nachury Maxence V MV
eLife 20200608
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<sup>GTP</sup>, and we describe the changes in BBSome conformation induced by ARL6<sup>GTP</sup> binding. Modeling the interactions of th ...[more]
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