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Originally published In Press as doi:10.1074/jbc.M201875200 on March 23, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19566-19572, May 31, 2002
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Polycystin-1 Activation of c-Jun N-terminal Kinase and AP-1 Is Mediated by Heterotrimeric G Proteins*

Stephen C. ParnellDagger §, Brenda S. MagenheimerDagger §, Robin L. MaserDagger , Christopher A. ZienDagger , Anna-Maria Frischauf, and James P. CalvetDagger ||

From the Dagger  Department of Biochemistry and Molecular Biology and the Kidney Institute, University of Kansas Medical Center, Kansas City, Kansas 66160 and  Institut fuer Genetik und Allgemeine Biologie, Universitaet Salzburg, A-5020 Salzburg, Austria

Functional analysis of polycystin-1, the product of the gene most frequently mutated in autosomal dominant polycystic kidney disease, has revealed that this protein is involved in the regulation of diverse signaling pathways such as the activation of the transcription factor AP-1 and modulation of Wnt signaling. However, the initial steps involved in the activation of such cascades have remained unclear. We demonstrated previously that the C-terminal cytosolic tail of polycystin-1 binds and activates heterotrimeric G proteins in vitro. To test if polycystin-1 can activate cellular signaling cascades via heterotrimeric G protein subunits, polycystin-1 C-terminal tail-mediated c-Jun N-terminal kinase (JNK) and AP-1 activities were assayed in transiently transfected 293T cells in the presence of dominant-negative, G protein inhibiting constructs, and in the presence of cotransfected Galpha subunits. The results showed that polycystin-1-mediated JNK/AP-1 activation is mediated by Galpha and Gbeta gamma subunits. Polycystin-1-mediated AP-1 activity could be significantly augmented by cotransfected Galpha i, Galpha q, and Galpha 12/13 subunits, suggesting that polycystin-1 can couple with and activate several heterotrimeric G protein families.

* This work was supported by National Institutes of Health Grants DK53763 (to J. P. C.) and DK57301 (to J. P. C. and R. L. M.), grants from the Polycystic Kidney Disease Foundation (to J. P. C. and R. L. M.), and a University of Kansas Medical Center Training Grant in Biomedical Research (to S. C. P.).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.

§ Both authors contributed equally to this work.

|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, KS 66160-7421. Tel.: 913-588-7424; Fax: 913-588-7440; E-mail: jcalvet@kumc.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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