The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.

Rud3p is a coiled-coil protein of the yeast cis-Golgi. We find that Rud3p is localized to the Golgi via a COOH-terminal domain that is distantly related to the GRIP domain that recruits several coiled-coil proteins to the trans-Golgi by binding the small Arf-like GTPase Arl1p. In contrast, Rud3p binds to ...
the GTPase Arf1p via this COOH-terminal "GRIP-related Arf-binding" (GRAB) domain. Deletion of RUD3 is lethal in the absence of the Golgi GTPase Ypt6p, and a screen of other mutants showing a similar genetic interaction revealed that Golgi targeting of Rud3p also requires Erv14p, a cargo receptor that cycles between the endoplasmic reticulum and Golgi. The one human protein with a GRAB domain, GMAP-210 (CEV14/Trip11/Trip230), is known to be on the cis-Golgi, but the COOH-terminal region that contains the GRAB domain has been reported to bind to centrosomes and gamma-tubulin (Rios, R.M, A. Sanchis, A.M. Tassin, C. Fedriani, and M. Bornens. 2004. Cell. 118:323-335). In contrast, we find that this region binds to the Golgi in a GRAB domain-dependent manner, suggesting that GMAP-210 may not link the Golgi to gamma-tubulin and centrosomes.
Mesh Terms:
ADP-Ribosylation Factor 1, Amino Acid Motifs, Amino Acid Sequence, Animals, COS Cells, Carrier Proteins, Chromatography, Endoplasmic Reticulum, GTP Phosphohydrolases, Gene Deletion, Genotype, Golgi Apparatus, Guanosine Diphosphate, Membrane Proteins, Microscopy, Confocal, Microscopy, Fluorescence, Microtubule-Associated Proteins, Molecular Sequence Data, Monomeric GTP-Binding Proteins, Mutation, Nuclear Proteins, Plasmids, Protein Conformation, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Tubulin, Vesicular Transport Proteins
J. Cell Biol.
Date: Oct. 25, 2004
Download Curated Data For This Publication
20140
Switch View:
  • Interactions 6