EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization

Michel Franco, Peter J. Peters, Joëlle Boretto, Elly Van Donselaar, Antonino Neri, Crislyn D'Souza-Schorey, Philippe Chavrier

Research output: Contribution to journalArticlepeer-review

Abstract

We have identified a human cDNA encoding a novel protein, exchange factor for ARF6 (EFA6), which contains Sec7 and pleckstrin homology domains. EFA6 promotes efficient guanine nucleotide exchange on ARF6 and is distinct from the ARNO family of ARF1 exchange factors. The protein localizes to a dense matrix on the cytoplasmic face of plasma membrane invaginations, induced on its expression. We show that EFA6 regulates endosomal membrane recycling and promotes the redistribution of transferrin receptors to the cell surface. Furthermore, expression of EFA6 induces actin-based membrane ruffles that are inhibited by co-expression of dominant-inhibitory mutant forms of ARF6 or Rac1. Our results demonstrate that by catalyzing nucleotide exchange on ARF6 at the plasma membrane and by regulating Rac1 activation, EFA6 coordinates endocytosis with cytoskeletal rearrangements.

Original languageEnglish
Pages (from-to)1480-1491
Number of pages12
JournalEMBO Journal
Volume18
Issue number6
Publication statusPublished - Mar 15 1999

Keywords

  • Actin
  • ARF6
  • Endocytosis
  • Guanine nucleotide exchange factor
  • Rac1

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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