Rho-specific binding and guanine nucleotide exchange catalysis by KIAA0380, a dbl family member.
Several guanine nucleotide exchange factors (GEFs) for Rho-GTPases have been identified, all of them containing a Dbl homology (DH) and pleckstrin homology (PH) domain, but exhibiting different specificities to the Rho family members, Rho, Rac and Cdc42. We report here that KIAA0380, a protein with a tandem DH/PH domain, an ... amino-terminal PDZ domain and a regulator of G protein signalling (RGS) homology domain, is a specific GEF for RhoA, but not for Rac1 and Cdc42, as determined by GDP release, guanosine 5'-O-(3-thio)triphosphate (GTPgammaS) binding and protein binding assays. When expressed in J82 cells, DH/PH domain-containing forms of KIAA0380 induced actin stress fibers, whereas expression of the RGS homology domain prevented lysophosphatidic acid (LPA)-induced stress fiber formation.
Mesh Terms:
Actins, Catalysis, Guanine Nucleotide Exchange Factors, Guanine Nucleotides, Humans, Molecular Sequence Data, Oligopeptides, Protein Conformation, Proto-Oncogene Proteins, Receptors, Cell Surface, Receptors, G-Protein-Coupled, Receptors, Lysophosphatidic Acid, Tumor Cells, Cultured, rhoA GTP-Binding Protein
Actins, Catalysis, Guanine Nucleotide Exchange Factors, Guanine Nucleotides, Humans, Molecular Sequence Data, Oligopeptides, Protein Conformation, Proto-Oncogene Proteins, Receptors, Cell Surface, Receptors, G-Protein-Coupled, Receptors, Lysophosphatidic Acid, Tumor Cells, Cultured, rhoA GTP-Binding Protein
FEBS Lett.
Date: Oct. 15, 1999
PubMed ID: 10526156
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