Regulation of RGS-RhoGEFs by Galpha12 and Galpha13 proteins.

by: S Tanabe, B Kreutz, N Suzuki, T Kozasa

Methods in enzymology, Vol. 390 (2004), pp. 285-294.

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Abstract

Three mammalian Rho guanine nucleotide exchange factors (RhoGEFs), leukemia-associated RhoGEF (LARG), p115RhoGEF, and PDZ-RhoGEF, contain regulator of G-protein signaling (RGS) domains within their amino-terminal regions. These RhoGEFs link signals from heterotrimeric G12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The activity of these RhoGEFs is regulated by Galpha12/13 through their RGS domains. Because RhoGEFs stimulate guanine nucleotide exchange by Rho GTPases, RhoGEF activation can be measured by monitoring GTP binding to or GDP dissociation from Rho GTPases. This article describes methods used to perform reconstitution assays to measure the activity of RhoGEFs regulated by Galpha12/13.

@article{citeulike:2805676, abstract = {Three mammalian Rho guanine nucleotide exchange factors (RhoGEFs), leukemia-associated RhoGEF (LARG), p115RhoGEF, and PDZ-RhoGEF, contain regulator of G-protein signaling (RGS) domains within their amino-terminal regions. These RhoGEFs link signals from heterotrimeric G12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The activity of these RhoGEFs is regulated by Galpha12/13 through their RGS domains. Because RhoGEFs stimulate guanine nucleotide exchange by Rho GTPases, RhoGEF activation can be measured by monitoring GTP binding to or GDP dissociation from Rho GTPases. This article describes methods used to perform reconstitution assays to measure the activity of RhoGEFs regulated by Galpha12/13.}, address = {Department of Pharmacology, University of Illinois at Chicago, 60612, USA.}, author = {Tanabe, S. and Kreutz, B. and Suzuki, N. and Kozasa, T. }, citeulike-article-id = {2805676}, doi = {http://dx.doi.org/10.1016/S0076-6879(04)90018-3}, issn = {0076-6879}, journal = {Methods in enzymology}, pages = {285--294}, posted-at = {2008-05-16 19:15:47}, priority = {2}, title = {Regulation of RGS-RhoGEFs by Galpha12 and Galpha13 proteins.}, url = {http://dx.doi.org/10.1016/S0076-6879(04)90018-3}, volume = {390}, year = {2004} }

RIS record

TY - JOUR ID - citeulike:2805676 L3 - citeulike-article-id:2805676 TI - Regulation of RGS-RhoGEFs by Galpha12 and Galpha13 proteins. JF - Methods in enzymology VL - 390 SP - 285 EP - 294 AD - Department of Pharmacology, University of Illinois at Chicago, 60612, USA. SN - 0076-6879 N2 - Three mammalian Rho guanine nucleotide exchange factors (RhoGEFs), leukemia-associated RhoGEF (LARG), p115RhoGEF, and PDZ-RhoGEF, contain regulator of G-protein signaling (RGS) domains within their amino-terminal regions. These RhoGEFs link signals from heterotrimeric G12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The activity of these RhoGEFs is regulated by Galpha12/13 through their RGS domains. Because RhoGEFs stimulate guanine nucleotide exchange by Rho GTPases, RhoGEF activation can be measured by monitoring GTP binding to or GDP dissociation from Rho GTPases. This article describes methods used to perform reconstitution assays to measure the activity of RhoGEFs regulated by Galpha12/13. AU - Tanabe, S AU - Kreutz, B AU - Suzuki, N AU - Kozasa, T PY - 2004/// UR - http://dx.doi.org/10.1016/S0076-6879(04)90018-3 ER -

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