4.6 Article

Larger than DbI: new structural insights into RhoA activation

Journal

TRENDS IN BIOCHEMICAL SCIENCES
Volume 30, Issue 4, Pages 163-165

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2005.02.002

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Funding

  1. NIGMS NIH HHS [GM65533, GM62299, GM57391] Funding Source: Medline

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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.

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