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The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia.

ABSTRACT: The BBSome is a complex of Bardet-Biedl Syndrome (BBS) proteins that shares common structural elements with COPI, COPII, and clathrin coats. Here, we show that the BBSome constitutes a coat complex that sorts membrane proteins to primary cilia. The BBSome is the major effector of the Arf-like GTPase Arl6/BBS3, and the BBSome and GTP-bound Arl6 colocalize at ciliary punctae in an interdependent manner. Strikingly, Arl6(GTP)-mediated recruitment of the BBSome to synthetic liposomes produces distinct patches of polymerized coat apposed onto the lipid bilayer. Finally, the ciliary targeting signal of somatostatin receptor 3 needs to be directly recognized by the BBSome in order to mediate targeting of membrane proteins to cilia. Thus, we propose that trafficking of BBSome cargoes to cilia entails the coupling of BBSome coat polymerization to the recognition of sorting signals by the BBSome.

SUBMITTER: Jin H

PROVIDER: S-EPMC2898735 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia.

Jin Hua H White Susan Roehl SR Shida Toshinobu T Schulz Stefan S Aguiar Mike M Gygi Steven P SP Bazan J Fernando JF Nachury Maxence V MV

Cell 20100601 7

The BBSome is a complex of Bardet-Biedl Syndrome (BBS) proteins that shares common structural elements with COPI, COPII, and clathrin coats. Here, we show that the BBSome constitutes a coat complex that sorts membrane proteins to primary cilia. The BBSome is the major effector of the Arf-like GTPase Arl6/BBS3, and the BBSome and GTP-bound Arl6 colocalize at ciliary punctae in an interdependent manner. Strikingly, Arl6(GTP)-mediated recruitment of the BBSome to synthetic liposomes produces distin ...[more]

PMID: 20603001

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Bardet-Biedl syndrome proteins control the cilia length through regulation of actin polymerization.

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