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-Structure paper
タイトル | Near-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年6月8日 |
著者 | Shuang Yang / Kriti Bahl / Hui-Ting Chou / Jonathan Woodsmith / Ulrich Stelzl / Thomas Walz / Maxence V Nachury / |
PubMed 要旨 | 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 ...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. |
リンク | Elife / PubMed:32510327 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.44 - 4.0 Å |
構造データ | EMDB-21251, PDB-6vnw: EMDB-21259, PDB-6voa: |
由来 |
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キーワード | PROTEIN TRANSPORT / Cilia / Bardet-Biedl Syndrome |