caa a22 4500 397556756 CHVBK 20180308164804.0 cr unu---uuuuu 161202e199608 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021401 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021401 Narumiya Shuh Department of Pharmacology, Kyoto University Faculty of Medicine, Sakyo-ku, Kyoto 606 The Small GTPase Rho: Cellular Functions and Signal Transduction [Elektronische Daten] [Shuh Narumiya] Rho, a Ras homologue of small GTPase, is present from yeast to mammals. It shuttles between the active GTP-bound form and the inactive GDP-bound form and works as a switch in stimulus-evoked cell adhesion and motility, enhancement of contractile responses, and cytokinesis. In these actions, Rho directs the reorganization of the actin cytoskeleton at a specific time and at a specific site in the cell. It also activates serum response factor possibly via a kinase cascade and mediates a growth signal to nuclei. Two signalling processes are known to lead to Rho activation: one is activation of certain types of G-protein-coupled receptors such as lysophosphatidic acid receptor, and the other is activation of other small GTPases including Ras, CDC42, and Rac. Molecules catalyzing the GDP-GTP exchange of Rho, Rho guanine nucleotide exchange factors (Rho GEF), and those catalyzing the acceleration of GTP hydrolysis, Rho GTPase activating proteins (Rho GAP), were identified as Dbl- and Bcr-containing molecules, respectively. In addition, a molecule inhibiting guanine nucleotide exchange of Rho, Rho guanine nucleotide dissociation inhibitor (Rho-GDI), was isolated and characterized. More recently, putative Rho targets possibly mediating various Rho actions have been identified by their selective interaction with GTP-bound Rho. They include lipid kinases such as phosphatidyl-inositol-5-kinase and protein serine/threonine kinases such as PKN and pl60ROCK. A model of the molecular mechanism of action of Rho constructed on the basis of these findings is presented. There are, however, still many unclarified links between cell stimulation, Rho activation and final Rho actions. © 1996 BY THE JOURNAL OF BIOCHEMISTRY JB Reviews nationallicence actin cytoskeleton nationallicence botulinum C3 exoenzyme nationallicence cell adhesion nationallicence GTPase nationallicence Rho nationallicence The Journal of Biochemistry Oxford University Press 120/2(1996-08), 215-228 0021-924X 120:2<215 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021401 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021401 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Narumiya Shuh Department of Pharmacology, Kyoto University Faculty of Medicine, Sakyo-ku, Kyoto 606 NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/2(1996-08), 215-228 0021-924X 120:2<215 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford