title: Signaling to the Rho GTPases: networking with the DH domain.
abstract: The Dbl homology (DH) domain was first identified in the Dbl oncogene product as the limit region required for mediating guanine nucleotide exchange on the Rho family GTPase Cdc42. Since the initial biochemical characterization of the DH domain, this conserved motif has been identified in a large family of proteins. In each case, a pleckstrin homology (PH) domain immediately follows the DH domain and this tandem DH-PH module is the signature motif of the Dbl family of guanine nucleotide exchange factors (GEFs). Recent structural studies have provided significant insight into the molecular basis of guanine nucleotide exchange by Dbl family GEFs, opening the door for understanding the specificity of the DH/GTPase interaction as well as providing a starting point for understanding how the exchange activity of these proteins is modulated to achieve specific biological outcomes in the cell.
authors.affiliation: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
authors.forename: Gregory R
authors.initials: GR
authors.lastname: Hoffman
authors.forename: Richard A
authors.initials: RA
authors.lastname: Cerione
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D005810:Multigene Family; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011519:Proto-Oncogenes; D015682:Retroviridae Proteins, Oncogenic / Q000737:chemistry / Q000235:genetics*; D015398:Signal Transduction; D020741:rho GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018909:src Homology Domains
chemical_list: D015682:Retroviridae Proteins, Oncogenic; D020741:rho GTP-Binding Proteins