Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
EMBO Rep. 2001 Mar;2(3):234-8.

The structural GDP/GTP cycle of human Arf6.

Author information

  • 1Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1, avenue de la Terrasse, 91198 Gif sur Yvette cedex and Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, 660 route des Lucioles, 06560 Valbonne, France.

Abstract

The small GTP-binding protein Arf6 coordinates membrane traffic at the plasma membrane with aspects of cytoskeleton organization. This function does not overlap with that of other members of the ADP-ribosylation factor (Arf) family, although their switch regions, which are their major sites of interaction with regulators and effectors, have virtually identical sequences. Here we report the crystal structure of full-length, non-myristoylated human Arf6 bound to GTPgammaS. Unlike their GDP-bound forms, the active forms of Arf6 and Arf1 are very similar. Thus, the switch regions are discriminatory elements between Arf isoforms in their inactive but not in their active forms, a property that may generalize to other families of small G proteins. This suggests that GTP-bound Arfs may establish specific interactions outside the switch regions and/or be recognized in their cellular context rather than as isolated proteins. The structure also allows further insight into the lack of spontaneous GTPase activity of Arf proteins.

PMID:
11266366
[PubMed - indexed for MEDLINE]
PMCID:
PMC1083839
Free PMC Article

Images from this publication.See all images (3)Free text

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk