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

J Cell Biol. 2004 Oct 25;167(2):281-92. doi: 10.1083/jcb.200407088.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP-Ribosylation Factor 1 / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Carrier Proteins / metabolism*
  • Chromatography
  • Cytoskeletal Proteins
  • Endoplasmic Reticulum / metabolism*
  • GTP Phosphohydrolases / metabolism*
  • Gene Deletion
  • Genotype
  • Golgi Apparatus / metabolism*
  • Guanosine Diphosphate / metabolism
  • Membrane Proteins / metabolism*
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • Microtubule-Associated Proteins / metabolism
  • Molecular Sequence Data
  • Monomeric GTP-Binding Proteins / metabolism
  • Mutation
  • Nuclear Proteins
  • Plasmids / metabolism
  • Protein Conformation
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Tubulin / metabolism
  • Vesicular Transport Proteins

Substances

  • Carrier Proteins
  • Cytoskeletal Proteins
  • Erv14 protein, S cerevisiae
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • RUD3 protein, S cerevisiae
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • TRIP11 protein, human
  • Tubulin
  • Vesicular Transport Proteins
  • Guanosine Diphosphate
  • GTP Phosphohydrolases
  • ADP-Ribosylation Factor 1
  • Monomeric GTP-Binding Proteins
  • YPT6 protein, S cerevisiae