Proteins containing Dbl homology (DH) domains activate Rho-family GTPases by functioning as specific guanine nucleotide exchange factors. All known DH domains have associated C-terminal pleckstrin homology (PH) domains that are implicated in targeting and regulatory functions. The crystal structure of ...
Canonical RhoGEFs are composed of two distinct domains, aDblhomology domain (DH), which catalyses the exchange of GDP for GTP in Rho GTPases, and aPlekstrinhomology domain (PH), which assists in localisation of GEFs and regulation of their activity (reviewed in15). Protein domain predictio...
Dbl homology (DH) domain is the signature of all Dbl family proteins and consists of around 200 residues (Table 1). In the majority of Dbl family proteins, the catalytic DH domain is followed by a pleckstrin homology (PH) domain of around 100 residues (Table 1) indicating its essential an...
This chapter describes the interaction of Ect2 and Dbl with Rho-related GTPases. The Ect2 and Dbl oncogenes encode proteins containing Dbl homology (DH) domains. The Ect2 oncogene was isolated as a transforming gene from the mouse epithelial cell line BALB/MK using cDNA cloning strategy. Tra...
the Dbl-homology (DH)-domain-deletion mutant of GEF115 inhibited Gα13- and Gα12-induced, but not GEF115 itself- or Gαq-induced, SRF activation... Junhao,Mao,Huidong,... - 《Proceedings of the National Academy of Sciences of the United States of America》 被引量: 178发表: 1998年...
Here, we describe a novel RhoGEF, denominated EhGEF3 from the parasite Entamoeba histolytica , which encodes a 110 kDa protein containing the domain arrangement of a Dbl homology domain in tandem with a pleckstrin homology domain, the DH domain of EhGEF3 is closely related with the one of ...
Dbl proteins possess a ∼200 residue catalytic Dbl-homology (DH) domain, that is arranged in tandem with a C-terminal pleckstrin homology (PH) domain in nearly all cases. Here we report the solution structure of the DH domain of human PAK-interacting exchange protein (βPIX). The domain ...
Proteins containing the Dbl homology (DH) domain are responsible for activating Rho GTPases by catalyzing the exchange of GDP for GTP. Receptor-initiated stimulation of Dbl protein Vav exchange activity involves tyrosine phosphorylation. We show through structure determination that the mVav1 DH domain...
This large family of proteins contains a catalytic Dbl homology (DH) domain in tandem with a pleckstrin homology (PH) domain. We investigated how the PH domain modulated the activity of Dbl. Our data showed that the Dbl PH domain binded to phosphatidylinositol phosphates, resulting in the ...
Abstract Guanine nucleotide exchange factors for Rho-GTPases (Rho-GEFs) invariably share a catalytic Dbl-Homology (DH) domain associated with a Pleckstrin Homology (PH) domain, whose function in Rho-GEF activation is not well understood. Trio is the first member of an emerging family of Dbl ...