Larger than Dbl: new structural insights into RhoA activation

Trends Biochem Sci. 2005 Apr;30(4):163-5. doi: 10.1016/j.tibs.2005.02.002.


Dbl homology (DH) domains are almost always followed immediately by pleckstrin homology (PH) domains in Dbl family proteins, and these DH-PH fragments directly activate GDP-bound Rho GTPases by catalyzing the exchange of GDP for GTP. New crystal structures of the DH-PH domains from leukemia-associated Rho guanine nucleotide exchange factor (RhoGEF) and PDZ-RhoGEF bound to RhoA reveal how DH-PH domains cooperate to specifically activate Rho GTPases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Enzyme Activation
  • Models, Molecular
  • Nucleotides, Cyclic / metabolism
  • Protein Structure, Tertiary*
  • rhoA GTP-Binding Protein / chemistry*
  • rhoA GTP-Binding Protein / metabolism*


  • Nucleotides, Cyclic
  • rhoA GTP-Binding Protein