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Papers In Press, published online ahead of print July 10, 2000
Department of Physiological Chemistry, University Medical Centre Utrecht, Utrecht 3584 CG
Corresponding Author: J.L.Bos{at}med.uu.nl
SUMMARY 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 GEF 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 localisation 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.
J. Biol. Chem, 10.1074/jbc.M001160200
Submitted on February 10, 2000
Revised on July 5, 2000
Accepted on July 10, 2000
RALGEF2, A PH domain containing guanine-nucleotide exchange factor for RAL
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