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Membrane curvature induced by Arf1-GTP is essential for vesicle formation.

The GTPase Arf1 is considered as a molecular switch that regulates binding and release of coat proteins that polymerize on membranes to form transport vesicles. Here, we show that Arf1-GTP induces positive membrane curvature and find that the small GTPase can dimerize dependent on GTP. Investigating a possible link between Arf dimerization and curvature formation, we isolated an Arf1 mutant that cannot dimerize. Although it was capable of exerting the classical role of Arf1 as a coat receptor, it could not mediate the formation of COPI vesicles from Golgi-membranes and was lethal when expressed in yeast. Strikingly, this mutant was not able to deform membranes, suggesting that GTP-induced dimerization of Arf1 is a critical step inducing membrane curvature during the formation of coated vesicles.

Pubmed ID: 18689681

Authors

  • Beck R
  • Sun Z
  • Adolf F
  • Rutz C
  • Bassler J
  • Wild K
  • Sinning I
  • Hurt E
  • Brügger B
  • Béthune J
  • Wieland F

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Data

August 19, 2008

Associated Grants

None

Mesh Terms

  • ADP-Ribosylation Factor 1
  • Animals
  • Dimerization
  • Golgi Apparatus
  • Guanosine Triphosphate
  • HeLa Cells
  • Humans
  • Intracellular Membranes
  • Lipid Metabolism
  • Liposomes
  • Models, Biological
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Rats