Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi.
A cellular role and the mechanism of action for small GTPase Arl1 have been defined. Arl1-GTP interacts with the GRIP domains of Golgin-97 and Golgin-245, a process dependent on conserved residues of the GRIP domains that are important for Golgi targeting. The switch II region of Arl1 confers the specificity ... of this interaction. Arl1-GTP mediates Golgi recruitment of Golgin-97 in a switch II-dependent manner, whereas tethering Arl1-GTP onto endosomes can mediate endosomal targeting of Golgin-97. Golgin-97 and Golgin-245 are dissociated from the Golgi when Arl1 is knocked-down by its siRNA. Arl1-GTP thus functions to recruit Golgin-97 and Golgin-245 onto the Golgi via interacting with their GRIP domains.
Mesh Terms:
ADP-Ribosylation Factors, Amino Acid Sequence, Autoantigens, Cells, Cultured, Cloning, Molecular, Humans, Membrane Proteins, Molecular Sequence Data, Peptides, Protein Binding, Protein Structure, Tertiary, RNA, Small Interfering, Sequence Analysis, Protein, Two-Hybrid System Techniques
ADP-Ribosylation Factors, Amino Acid Sequence, Autoantigens, Cells, Cultured, Cloning, Molecular, Humans, Membrane Proteins, Molecular Sequence Data, Peptides, Protein Binding, Protein Structure, Tertiary, RNA, Small Interfering, Sequence Analysis, Protein, Two-Hybrid System Techniques
Mol. Biol. Cell
Date: Sep. 01, 2003
PubMed ID: 12972563
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