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Published 27 May 2003. doi:10.1083/jcb.200211094
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© The Rockefeller University Press, 0021-9525/2003/5/769 $5.00
The Journal of Cell Biology, Volume 161, Number 4, 769-777

Article

Dishevelled activates Ca2+ flux, PKC, and CamKII in vertebrate embryos



Laird C. Sheldahl1, Diane C. Slusarski2, Petra Pandur3, Jeffrey R. Miller4, Michael Kühl3 and Randall T. Moon1

1 Howard Hughes Medical Institute, Department of Pharmacology, and Center for Developmental Biology, University of Washington School of Medicine, Seattle, WA 98195
2 Department of Biological Sciences, University of Iowa, Iowa City, IA 52242
3 Abteilung für Biochemie, Universität Ulm, 89069 Ulm, Germany
4 University of Minnesota, Minneapolis, MN 55455

Address correspondence to Randall T. Moon, Dept. of Pharmacology, Campus Box 357750, University of Washington School of Medicine, Seattle, WA 98195. Tel.: (206) 543-1722. Fax: (206) 543-0858. E-mail: rtmoon{at}u.washington.edu

Wnt ligands and Frizzled (Fz) receptors have been shown to activate multiple intracellular signaling pathways. Activation of the Wnt–ß-catenin pathway has been described in greatest detail, but it has been reported that Wnts and Fzs also activate vertebrate planar cell polarity (PCP) and Wnt–Ca2+ pathways. Although the intracellular protein Dishevelled (Dsh) plays a dual role in both the Wnt–ß-catenin and the PCP pathways, its potential involvement in the Wnt–Ca2+ pathway has not been investigated. Here we show that a Dsh deletion construct, XDsh{Delta}DIX, which is sufficient for activation of the PCP pathway, is also sufficient for activation of three effectors of the Wnt–Ca2+ pathway: Ca2+ flux, PKC, and calcium/calmodulin-dependent protein kinase II (CamKII). Furthermore, we find that interfering with endogenous Dsh function reduces the activation of PKC by Xfz7 and interferes with normal heart development. These data suggest that the Wnt–Ca2+ pathway utilizes Dsh, thereby implicating Dsh as a component of all reported Fz signaling pathways.

Key Words: Dishevelled; PKC; Wnt; calcium; signal transduction

L.C. Sheldahl's present address is Department of Cell and Developmental Biology, Oregon Health Sciences University, Portland, OR 97201.

* Abbreviations used in this paper: CamKII, calcium/calmodulin-dependent protein kinase II; Dsh, Dishevelled; Fz, Frizzled; JNK, jun-N-terminal kinase; MO, morpholino; PCP, planar cell polarity; PTX, pertussis toxin; TnIc, cardiac troponin I; wt, wild type.


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