Extracellular Signal-Regulated Kinase Promotes Rho-Dependent Focal Adhesion Formation by Suppressing p190A RhoGAP
Author:
Affiliation:
1. Department of Pharmacology
2. Stanley Scott Cancer Center, School of Medicine, Louisiana State University Health Sciences Center, New Orleans, Louisiana
Abstract
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Link
https://journals.asm.org/doi/pdf/10.1128/MCB.01178-09
Reference90 articles.
1. Aktories, K., and I. Just. 1995. In vitro ADP-ribosylation of Rho by bacterial ADP-ribosyltransferases. Methods Enzymol.256:184-195.
2. Amano, M., K. Chihara, K. Kimura, Y. Fukata, N. Nakamura, Y. Matsuura, and K. Kaibuchi. 1997. Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science275:1308-1311.
3. Amano, M., H. Mukai, Y. Ono, K. Chihara, T. Matsui, Y. Hamajima, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996. Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science271:648-650.
4. Arthur, W. T., and K. Burridge. 2001. RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell12:2711-2720.
5. Arthur, W. T., L. A. Petch, and K. Burridge. 2000. Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol.10:719-722.
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