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Structure and Function of p63RhoGEF, a Gα q Activated Effector
Author(s) -
Taylor Veronica G,
Boguth Cassandra A,
Miller Brittney,
Cierpicki Tomasz,
Tesmer John J G
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.lb404
Subject(s) - heterotrimeric g protein , rhoa , guanine nucleotide exchange factor , effector , chemistry , regulator , microbiology and biotechnology , g protein , biology , signal transduction , biochemistry , gene
RhoA, a key actin cytoskeleton regulator, is activated in response to G protein‐coupled receptors signaling through Gα q . Rho guanine nucleotide exchange factor (RhoGEF) p63RhoGEF, a member of the Dbl GEF family, is directly activated by Gα q . Although the atomic structure of the Gα q ‐p63RhoGEF complex is known, the mechanism of activation is not clear, in part because the structure for the basal conformation of p63RhoGEF has not yet been determined. This poster describes our efforts to use nuclear magnetic resonance spectroscopy to determine the solution structure of the p63RhoGEF catalytic core, to map the residues directly interacting with RhoA in the presence and absence of Gα q , and to confirm the multi‐domain interactions of Gα q that were observed in the original crystal structure. The successful completion of this work would be the first example of a heterotrimeric G protein effector characterized in both its basal and activated states, and provide the molecular basis for regulation of an important link between heterotrimeric and small molecular weight G proteins. Support was provided by NIH grants HL071818 and HL086865.