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- Title
Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1.
- Authors
Mousheng Wu, Stephen C.; Lei Lu, Stephen C.; Wanjin Hong; Haiwei Song, Stephen C.
- Abstract
Recruitment of the GRIP domain golgins to the trans-Golgi network is mediated by Arl1, a member of the ARF/Arl small GTPase family, through interaction between their GRIP domains and Arl1-GTP. The crystal structure of Arl1-GTP in complex with the GRIP domain of golgin-245 shows that Arl1-GTP interacts with the GRIP domain predominantly in a hydrophobic manner, with the switch II region conferring the main recognition surface. The involvement of the switch and interswitch regions in the interaction between Arl1-GTP and GRIP accounts for the specificity of GRIP domain for Arl1-GTP. Mutations that abolished the Arl1-mediated Golgi localization of GRIP domain golgins have been mapped on the interface between Arl1-GTP and GRIP. Notably, the GRIP domain forms a homodimer in which each subunit interacts separately with one Arl1-GTP. Mutations disrupting the GRIP domain dimerization also abrogated its Golgi targeting, suggesting that the dimeric form of GRIP domain is a functional unit.
- Subjects
GOLGI apparatus; GUANOSINE triphosphate; ORGANELLES; GENE targeting; DIMERS; MOLECULAR biology
- Publication
Nature Structural & Molecular Biology, 2004, Vol 11, Issue 1, p86
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb714