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Papers In Press, published online ahead of print January 13, 2003
Department of Biochemistry, The Howard Hughes Medical Institute, Dallas, TX 75390-9050
Corresponding Author: stephen.sprang{at}utsouthwestern.edu
Structural requirements for function of the rgRGS domains of p115RhoGEF and homologous exchange factors differ from those of the classical RGS domains. An extensive mutagenesis analysis of the p115RhoGEF rgRGS domain was undertaken to determine its functional interface with the Galpha13 subunit. Results indicate that there is global resemblance between the interaction surface of the rgRGS domain with Galpha13 and the interactions of RGS4 and RGS9 with their Galpha substrates. However, there are distinct differences in the distribution of functionally critical residues between these structurally similar surfaces and an additional essential requirement for a cluster of negatively charged residues at the N-terminus of rgRGS. Lack of sequence conservation within the N-terminus may also explain the lack of GAP activity in a subset of the rgRGS domains. For all mutations, loss of functional GAP activity is paralleled by decreases in binding to Galpha13. The same mutations, when placed in the context of the p115RhoGEF molecule, produce deficiencies in GAP activity as observed with the rgRGS domain alone but show no attenuation of the regulation of Rho exchange activity by Galpha13. This suggests that the rgRGS domain may serve a structural or allosteric role in the regulation of the nucleotide exchange activity of p115RhoGEF on Rho by Galpha13.
J. Biol. Chem, 10.1074/jbc.M212695200
Submitted on December 12, 2002
Revised on January 13, 2003
Accepted on January 13, 2003
Mapping the G
13 binding interface of the rgRGS domain of p115RhoGEF
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