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The Conserved Bardet-Biedl Syndrome Proteins Assemble a Coat that Traffics Membrane Proteins to Cilia
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Summary 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. Biochemically, the BBSome is the major effector of the Arf-like GTPase Arl6/ BBS3. In vivo, the BBSome and Arl6 localize to ciliary punctae and Arl6GTP is required to target the BBSome to cilia. Congruently, GTP-bound Arl6 and acidic phospholipids are sufficient to efficiently recruit the BBSome to chemically defined liposomes. Finally, ultrastructural analyses demonstrate that BBSome binding to liposomes produces distinct patches of polymerized coat. Since we establish that the ciliary targeting signal of somatostatin receptor 3 needs to be directly recognized by the BBSome to mediate targeting to cilia, we propose that trafficking to cilia entails the coupling of BBSome coat polymerization to the recognition of sorting signals.
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Metadata
- Authors
- Jin, H., White, S. R., Shida, T., Schulz, S., Aguiar, M., Gygi, S. P., Bazan, J. F., & Nachury, M. V.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 141
- Issue
- 7
- Pages
- 1208-1219
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2161570516
- Cited by
- 605
- References
- 6
- FWCI
- 29.17
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1178 d)
- Funders
- March of Dimes Foundation (5-FY09-112)
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM089933, BR-5014, F32GM089218)
- American Heart Association (AHA-0930365N)
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