RalGEF2, a pleckstrin homology domain containing guanine nucleotide exchange factor for Ral.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Blood Proteins, COS Cells, Enzyme Activation, Molecular Sequence Data, Phosphoproteins, Sequence Alignment, Substrate Specificity, ral GTP-Binding Proteins, ral Guanine Nucleotide Exchange Factor
Amino Acid Sequence, Animals, Blood Proteins, COS Cells, Enzyme Activation, Molecular Sequence Data, Phosphoproteins, Sequence Alignment, Substrate Specificity, ral GTP-Binding Proteins, ral Guanine Nucleotide Exchange Factor
J. Biol. Chem.
Date: Sep. 22, 2000
PubMed ID: 10889189
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