P-Rex2, a new guanine-nucleotide exchange factor for Rac
| Autor: | Simon Andrews, Sarah Donald, Heidi C.E. Welch, Kirsti Hill, Simon Walker, Charlotte Lécureuil, Romain Barnouin, Sonja Krugmann, Len R. Stephens, Phillip T. Hawkins, W. John Coadwell |
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| Rok vydání: | 2004 |
| Předmět: |
Protein subunit
Biophysics P-Rex2 P-Rex1 Inositol 1 4 5-Trisphosphate PI3K Biochemistry chemistry.chemical_compound Structural Biology Heterotrimeric G protein Genetics Humans Small GTPase Phosphatidylinositol Cloning Molecular GEF Receptor Molecular Biology PI3K/AKT/mTOR pathway Gene Library Chemistry Cell Biology Blotting Northern Heterotrimeric GTP-Binding Proteins Recombinant Proteins rac GTP-Binding Proteins Rac Cell biology Rac GTP-Binding Proteins Protein Subunits Organ Specificity Guanine nucleotide exchange factor Gβγ subunits |
| Zdroj: | FEBS Letters. 572:172-176 |
| ISSN: | 0014-5793 |
| Popis: | We have identified a new guanine-nucleotide exchange factor, P-Rex2, and cloned it from human skeletal muscle and brain libraries. It has widespread tissue distribution but is not expressed in neutrophils. P-Rex2 is a 183 kDa protein that activates the small GTPase Rac and is regulated by phosphatidylinositol (3,4,5)-trisphosphate and the beta gamma subunits of heterotrimeric G proteins in vitro and in vivo. P-Rex2 has structure, activity and regulatory properties similar to P-Rex1 but has divergent tissue distribution, as P-Rex1 is mainly expressed in neutrophils. Together, they form an enzyme family capable of mediating Rac signalling downstream of G protein-coupled receptors and phosphoinositide 3-kinase. |
| Databáze: | OpenAIRE |
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