A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements

Crislyn D'Souza-Schorey*, Rita L. Boshans, Michelle McDonough, Philip D. Stahl, Linda Van Aelst

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

196 Scopus citations


The ARF6 GTPase, the least conserved member of the ADP ribosylation factor (ARF) family, associates with the plasma membrane and intracellular endosome vesicles. Mutants of ARF6 defective in GTP binding and hydrolysis have a marked effect on endocytic trafficking and the gross morphology of the peripheral membrane system. Here we report that expression of the GTPase-defective mutant of ARF6, ARF6(Q67L), remodels the actin cytoskeleton by inducing actin polymerization at the cell periphery. This cytoskeletal rearrangement was inhibited by co-expression of ARF6(Q67L) with deletion mutants of POR1, a Rac1-interacting protein involved in membrane ruffling, but not with the dominant-negative mutant of Rac1, Rac1(S17N). A synergistic effect between POR1 and ARF6 for the induction of actin polymerization was detected. Furthermore, we observed that ARF6 interacts directly with POR1 and that this interaction was GTP dependent. These findings indicate that ARF6 and Rac1 function on distinct signaling pathways to mediate cytoskeletal reorganization, and suggest a role for POR1 as an important regulatory element in orchestrating cytoskeletal rearrangements at the cell periphery induced by ARF6 and Rac1.

Original languageEnglish (US)
Pages (from-to)5445-5454
Number of pages10
JournalEMBO Journal
Issue number17
StatePublished - Sep 1 1997


  • ARF6
  • Cytoskeletal rearrangements
  • POR1
  • Rac

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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