Structure of the Sec7 domain of the Arf exchange factor ARNO

Jacqueline Cherfils (), Julie Ménétrey, Magali Mathieu, Gérard Le Bras, Sylviane Robineau, Sophie Béraud-Dufour, Bruno Antonny and Pierre Chardin
Additional contact information
Jacqueline Cherfils: Laboratoire d'Enzymologie et Biochimie Structurales
Julie Ménétrey: Laboratoire d'Enzymologie et Biochimie Structurales
Magali Mathieu: Laboratoire d'Enzymologie et Biochimie Structurales
Gérard Le Bras: Laboratoire d'Enzymologie et Biochimie Structurales
Sylviane Robineau: Institut de Pharmacologie Moléculaire et Cellulaire du CNRS-UPR 411
Sophie Béraud-Dufour: Institut de Pharmacologie Moléculaire et Cellulaire du CNRS-UPR 411
Bruno Antonny: Institut de Pharmacologie Moléculaire et Cellulaire du CNRS-UPR 411
Pierre Chardin: Institut de Pharmacologie Moléculaire et Cellulaire du CNRS-UPR 411

Nature, 1998, vol. 392, issue 6671, 101-105

Abstract: Abstract Small G proteins switch from a resting, GDP-bound state to an active, GTP-bound state. As spontaneous GDP release is slow, guanine-nucleotide-exchange factors (GEFs) are required to promote fast activation of small G proteins through replacement of GDP with GTP in vivo1. Families of GEFs with no sequence similarity to other GEF families have now been assigned to most families of small G proteins. In the case of the small G protein Arf1, the exchange of bound GDP for GTP promotes the coating of secretory vesicles in Golgi traffic2. An exchange factor for human Arf1, ARNO3, and two closely related proteins, named cytohesin 1 (ref. 4) and GPS1 (ref. 5), have been identified. These three proteins are modular proteins with an amino-terminal coiled-coil, a central Sec7-like domain and a carboxy-terminal pleckstrin homology domain. The Sec7 domain contains the exchange-factor activity3. It was first found in Sec7, a yeast protein involved in secretion6, and is present in several other proteins, including the yeast exchange factors for Arf, Gea1 and Gea2 (7–9). Here we report the crystal structure of the Sec7 domain of human ARNO at 2 Å resolution and the identification of the site of interaction of ARNO with Arf.

Date: 1998
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DOI: 10.1038/32210

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