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J. Biol. Chem., Vol. 275, Issue 38, 29761-29766, September 22, 2000
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From the Ral is a ubiquitously expressed Ras-like small
GTPase. Several guanine nucleotide exchange factors for Ral have been
identified, including members of the RalGDS family, which exhibit a Ras
binding domain and are regulated by binding to RasGTP. Here we describe a novel type of RalGEF, RalGEF2. This guanine nucleotide exchange factor has a characteristic Cdc25-like catalytic domain at the N
terminus and a pleckstrin homology (PH) domain at the C terminus. RalGEF2 is able to activate Ral both in vivo and in
vitro. Deletion of the PH domain results in an increased
cytoplasmic localization of the protein and a corresponding reduction
in activity in vivo, suggesting that the PH domain
functions as a membrane anchor necessary for optimal activity in
vivo.
Department of Physiological Chemistry and
Centre for Biomedical Genetics, University Medical Centre Utrecht,
Universiteitsweg 100, 3584 CG Utrecht, The Netherlands and the
¶ Abteilung Strukturelle Biologie, Max-Planck-Institut für
Molekulare Physiologie, Otto-Hahn-Straße 11, 44227 Dortmund, Germany
Present address: Dept. of Molecular Microbiology, Groningen
University, 9750 AA Haren, The Netherlands.
**
To whom correspondence should be addressed. Tel.: 31-30-253-89-77;
Fax: 31-30-253-90-35; E-mail: j.l.bos@med.uu.nl.
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