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Protein–protein‐interactions in a multiplexed, miniaturized format a functional analysis of Rho GTPase activation and inhibition
Author(s) -
Schmohl Michael,
Rimmele Stefanie,
Pötz Oliver,
Kloog Yoel,
Gierschik Peter,
Joos Thomas O.,
SchneiderhanMarra Nicole
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900597
Subject(s) - gtpase , gtp' , protein–protein interaction , chemistry , microbiology and biotechnology , gtp binding protein regulators , gtpase activating protein , biochemistry , biophysics , g protein , biology , signal transduction , enzyme
Abstract A miniaturized, bead‐based protein–protein‐interaction assay was developed to study the interaction of Rho GTPases with regulatory proteins. The setup, which uses only minute amounts of sample, was used to analyze small molecules that inhibit the interaction between Rho GTPases and RhoGDIα. Prenylcysteine analogues and the replacement of GDP by non‐hydrolysable GTP analogues prevented the formation of Rho GTPase‐RhoGDIα complexes in a concentration‐dependent manner.