Structure of Gα<subscript>q</subscript>-p63RhoGEF-RhoA Complex Reveals a Pathway for the Activation of RhoA by GPCRs.
In: Science, Jg. 318 (2007-12-21), Heft 5858, S. 1923-1927
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Zugriff:
The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric guanine nucleotide-binding protein (G protein) Gαq and thereby links Gag-coupled receptors (GPCRs) to the activation of the small-molecular-weight G protein RhoA. We determined the crystal structure of the Gαq- p63RhoGEF-RhoA compLex, detailing the interactions of Gαq with the Dbl and pteckstrin homology (DH and PH) domains of p63RhoGEF. These interactions involve the effector-binding site and the C-terminaL region of Gαq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Gαq effectors that appear to activate RhoA both in vitro and in intact cells. We propose that this structure represents the crux of an ancient signal transduction pathway that is expected to be important in an array of physiological processes. [ABSTRACT FROM AUTHOR]
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Structure of Gα<subscript>q</subscript>-p63RhoGEF-RhoA Complex Reveals a Pathway for the Activation of RhoA by GPCRs.
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Autor/in / Beteiligte Person: | Lutz, Susanne ; Shankaranarayanan, Aruna ; Coco, Cassandra ; Ridilla, Marc ; Nance, Mark R. ; Vettel, Christiane ; Baltus, Doris ; Evelyn, Chris R. ; Neubig, Richard R. ; Wieiand, Thomas ; Tesmer, John J. G. |
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Zeitschrift: | Science, Jg. 318 (2007-12-21), Heft 5858, S. 1923-1927 |
Veröffentlichung: | 2007 |
Medientyp: | academicJournal |
ISSN: | 0036-8075 (print) |
DOI: | 10.1126/science.1147554 |
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