Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1.

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.
Mesh Terms:
ADP-Ribosylation Factors, Amino Acid Sequence, Animals, Autoantigens, Binding Sites, Crystallography, X-Ray, Dimerization, GTP Phosphohydrolases, Humans, In Vitro Techniques, Macromolecular Substances, Membrane Proteins, Models, Biological, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Rats, Recombinant Proteins, Sequence Homology, Amino Acid, trans-Golgi Network
Nat. Struct. Mol. Biol.
Date: Jan. 01, 2004
Download Curated Data For This Publication
215224
Switch View:
  • Interactions 4