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Originally published In Press as doi:10.1074/jbc.M102450200 on March 28, 2001

J. Biol. Chem., Vol. 276, Issue 25, 22003-22010, June 22, 2001
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Angiotensin II-induced Stimulation of p21-activated Kinase and c-Jun NH2-terminal Kinase Is Mediated by Rac1 and Nck*

Udo SchmitzDagger , Kerstin Thömmes, Imke Beier, Wolfgang Wagner, Agapios Sachinidis, Rainer Düsing, and Hans Vetter

From the Medizinische Universitäts-Poliklinik, Wilhelmstrasse 35-37, 53111 Bonn, Germany

p21-activated kinase (PAK) has been shown to be an upstream mediator of JNK in angiotensin II (AngII) signaling. Little is known regarding other signaling molecules involved in activation of PAK and JNK by AngII. Rho family GTPases Rac and Cdc42 have been shown to enhance PAK activity by binding to p21-binding domain of PAK (PAK-PBD). In vascular smooth muscle cells (VSMC) AngII stimulated Rac1 binding to GST-PAK-PBD fusion protein. Pretreatment of VSMC by genistein inhibited AngII-induced Rac1 activation, whereas Src inhibitor PP1 had no effect. Inhibition of protein kinase C by phorbol 12,13-dibutyrate pretreatment also decreased AngII-mediated activation of Rac1. The adaptor molecule Nck has been shown previously to mediate PAK activation by facilitating translocation of PAK to the plasma membrane. In VSMC AngII stimulated translocation of Nck and PAK to the membrane fraction. Overexpression of dominant-negative Nck in Chinese hamster ovary (CHO) cells, stably expressing the AngII type I receptor (CHO-AT1), inhibited both PAK and JNK activation by AngII, whereas it did not affect ERK1/2. Finally, dominant-negative Nck inhibited AngII-induced DNA synthesis in CHO-AT1 cells. Our data provide evidence for Rac1 and Nck as upstream mediators of PAK and JNK in AngII signaling and implicate JNK in AngII-induced growth responses.

* This work was supported by the German Research Foundation Grant SCHM 1174/3-1 (to U. S.) and by the BONFOR Program Grant BONFOR 110/24 (to K. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Medizinische Universitäts-Poliklinik, Wilhelmstrasse 35-37, 53111 Bonn, Germany. Tel.: 49-228-287-2263; Fax: 49-228-287-2658; E-mail: uschmitz@uni- bonn.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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