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RalGEF2, a pleckstrin homology domain containing guanine nucleotide exchange factor for Ral.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2000 Sep 22; Vol. 275 (38), pp. 29761-6. - Publication Year :
- 2000
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Blood Proteins genetics
Blood Proteins metabolism
COS Cells
Enzyme Activation
Molecular Sequence Data
Phosphoproteins genetics
Phosphoproteins metabolism
Sequence Alignment
Substrate Specificity
ral Guanine Nucleotide Exchange Factor genetics
ral GTP-Binding Proteins metabolism
ral Guanine Nucleotide Exchange Factor analysis
ral Guanine Nucleotide Exchange Factor metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 275
- Issue :
- 38
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 10889189
- Full Text :
- https://doi.org/10.1074/jbc.M001160200