Larger than Dbl: new structural insights into RhoA activation

Kent L Rossman; John Sondek

doi:10.1016/j.tibs.2005.02.002

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.

Authors

Kent L Rossman¹, John Sondek

Affiliation

¹ Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

PMID: 15817389
DOI: 10.1016/j.tibs.2005.02.002

Abstract

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*

Substances

Nucleotides, Cyclic
rhoA GTP-Binding Protein

Abstract

Publication types

MeSH terms

Substances

Grants and funding