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FEBS Lett. 1999 Oct 15;459(3):313-8.

Rho-specific binding and guanine nucleotide exchange catalysis by KIAA0380, a dbl family member.

Author information

1
Institut für Pharmakologie, Universitätsklinikum Essen, Hufelandstr. 55, D-45122, Essen, Germany. ulrich.ruemenapp@uni-essen.de

Erratum in

  • FEBS Lett 2000 Feb 4;467(1):134-5.

Abstract

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.

PMID:
10526156
DOI:
10.1016/s0014-5793(99)01270-3
[Indexed for MEDLINE]
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