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

Mousheng Wu; Lei Lu; Wanjin Hong; Haiwei Song

doi:10.1038/nsmb714

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

Nat Struct Mol Biol. 2004 Jan;11(1):86-94. doi: 10.1038/nsmb714. Epub 2003 Dec 29.

Authors

Mousheng Wu¹, Lei Lu, Wanjin Hong, Haiwei Song

Affiliation

¹ Laboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609.

PMID: 14718928
DOI: 10.1038/nsmb714

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

ADP-Ribosylation Factors*
Amino Acid Sequence
Animals
Autoantigens / chemistry*
Autoantigens / genetics
Autoantigens / metabolism*
Binding Sites
Crystallography, X-Ray
Dimerization
GTP Phosphohydrolases / chemistry*
GTP Phosphohydrolases / genetics
GTP Phosphohydrolases / metabolism*
Humans
In Vitro Techniques
Macromolecular Substances
Membrane Proteins / chemistry*
Membrane Proteins / genetics
Membrane Proteins / metabolism*
Models, Biological
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Rats
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Sequence Homology, Amino Acid
trans-Golgi Network / metabolism

Substances

Autoantigens
GOLGA4 protein, human
Macromolecular Substances
Membrane Proteins
Recombinant Proteins
ADP-ribosylation factor related proteins
GTP Phosphohydrolases
ADP-Ribosylation Factors