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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.

Pubmed ID: 12972563


  • Lu L
  • Hong W


Molecular biology of the cell

Publication Data

September 15, 2003

Associated Grants


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