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The Role Of P115 Rhogef In The Rho Mediated Effects Of Lpa On The Actin Cytoskeleton.

Published online by Cambridge University Press:  02 July 2020

C.L. Schwartz
Affiliation:
The Dept. of Biology, The University of Texas at Arlington, Arlington, TX76019 The Depts.of Anesthesiology and Pharmacology, Southwestern Medical Center at Dallas, Dallas, TX75235.
C. Wells
Affiliation:
The Depts.of Anesthesiology and Pharmacology, Southwestern Medical Center at Dallas, Dallas, TX75235.
X. Jiang
Affiliation:
The Depts.of Anesthesiology and Pharmacology, Southwestern Medical Center at Dallas, Dallas, TX75235.
H.J. Arnott
Affiliation:
The Dept. of Biology, The University of Texas at Arlington, Arlington, TX76019
P.C. Sternweis
Affiliation:
The Depts.of Anesthesiology and Pharmacology, Southwestern Medical Center at Dallas, Dallas, TX75235.
M. A. Wilk-Blaszczak
Affiliation:
The Depts.of Anesthesiology and Pharmacology, Southwestern Medical Center at Dallas, Dallas, TX75235.
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Extract

In the fibroblast cell line, 3T3, lysophosphatidic acid (LPA) induces stress fiber formation. Stress fibers participate in physiological functions such as cell motility. LPA acts through a receptor coupled to a PTX-insensitive G-protein, G13. It was shown that a constitutively activated mutant of α13 (Q226L) induces stress fiber formation in Swiss3T3 cells through a second messenger cascade that involves a monomeric G-protein, Rho. The recently discovered guanine nucleotide exchange factor, p115 RhoGEF (p115) forms a link between a n and Rho A. In the presence of α13, p115 activates Rho. The N-terminus of p115 contains a regulator of G-protein signaling (RGS) box. RGS proteins act as negative regulators of G-protein dependent signaling by increasing GTPase activity and “locking” the G-protein in an inactive state. We have tested a role of p115 in the pathway coupling the LPA receptor to stress fiber formation by Rho in NTH-3T3 cells.

Type
Cytochemistry
Copyright
Copyright © Microscopy Society of America

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