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J. Biol. Chem., Vol. 282, Issue 44, 31873-31881, November 2, 2007

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A Novel Tyrosine Phosphorylation Site in Protein Kinase D Contributes to Oxidative Stress-mediated Activation^*

From the Department of Cancer Biology, Mayo Clinic Comprehensive Cancer Center, Jacksonville, Florida 32224

Protein kinase D1 (PKD1) is a mediator of oxidative stress signaling where it regulates cellular detoxification and survival. Critical for the regulation of PKD1 activity in response to oxidative stress are Src- and Abl-mediated tyrosine phosphorylations that eventually lead to protein kinase C (PKC)-mediated activation of PKD1. Here we identify Tyr⁹⁵ in PKD1 as a previously undescribed phosphorylation site that is regulated by oxidative stress. Our data suggest that PKD1 phosphorylation at Tyr⁹⁵ generates a binding motif for PKC, and that oxidative stress-mediated PKC/PKD interaction results in PKD1 activation loop phosphorylation and activation. We further analyzed all PKD isoforms for this mechanism and show that PKD enzymes PKD1 and PKD2 are targets for PKC in response to oxidative stress, and that PKD3 is not a target because it lacks the relevant tyrosine residue that generates a PKC interaction motif.

Received for publication, April 30, 2007 , and in revised form, August 17, 2007.

^* This work was supported by the Mayo Foundation and the Mayo Comprehensive Cancer Center. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

¹ To whom correspondence should be addressed: Griffin Rm. 306, 4500 San Pablo Rd., Jacksonville, FL 32224. Tel.: 904-953-6909; Fax: 904-953-0277; E-mail: storz.peter{at}mayo.edu.

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