期刊
TRAFFIC
卷 18, 期 11, 页码 720-732出版社
WILEY
DOI: 10.1111/tra.12507
关键词
Caenorhabditis elegans; coiled-coil domain; dense-core vesicle; golgin; GTPase; insulinoma 832; 13 cells; lipid binding protein; membrane trafficking; Rab
类别
资金
- NIH Institutional Training Grant for Neurobiology [T32 GM007108]
- University of Washington Diabetes Research Center Pilot and Feasibility Award, NIH [P30 DK017047]
- NIH [R01 GM077349, R00 MH082109]
- Ellison Medical Foundation New Scholar Award
Dense-core vesicles (DCVs) are secretory organelles that store and release modulatory neurotransmitters from neurons and endocrine cells. Recently, the conserved coiled-coil protein CCCP-1 was identified as a component of the DCV biogenesis pathway in the nematode Caenorhabditis elegans. CCCP-1 binds the small GTPase RAB-2 and colocalizes with it at the trans-Golgi. Here, we report a structure-function analysis of CCCP-1 to identify domains of the protein important for its localization, binding to RAB-2, and function in DCV biogenesis. We find that the CCCP-1 C-terminal domain (CC3) has multiple activities. CC3 is necessary and sufficient for CCCP-1 localization and for binding to RAB-2, and is required for the function of CCCP-1 in DCV biogenesis. In addition, CCCP-1 binds membranes directly through its CC3 domain, indicating that CC3 may comprise a previously uncharacterized lipid-binding motif. We conclude that CCCP-1 is a coiled-coil protein that binds an activated Rab and localizes to the Golgi via its C-terminus, properties similar to members of the golgin family of proteins. CCCP-1 also shares biophysical features with golgins; it has an elongated shape and forms oligomers.
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