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J. Biol. Chem., Vol. 281, Issue 40, 29711-29718, October 6, 2006

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The Tyrosine Kinase c-Abl Protects c-Jun from Ubiquitination-mediated Degradation in T Cells^*

Beixue Gao, Sang-Myeong Lee, and Deyu Fang¹

From the Departments of Otolaryngology-Head and Neck Surgery and Molecular Microbiology and Immunology, University of Missouri-Columbia School of Medicine, Columbia, Missouri 65212

The cross-talk of ubiquitination with other types of posttranscriptional modifications, such as phosphorylation, regulates the stability of many proteins. We have previously demonstrated that c-Jun is a substrate of Itch, a HECT-type E3 ubiquitin ligase. c-Jun is also a substrate of the tyrosine kinase c-Abl. Here we report that genetic ablation of c-Abl accelerated c-Jun degradation. Phosphorylation of the tyrosine within the PPXY motif by c-Abl inhibited c-Jun ubiquitination and its binding by Itch. The nuclear localization of c-Abl, triggered by T-cell activation signals, was essential for its activity in regulating c-Jun transcription activity. These findings define a potential molecular mechanism for the immunodeficiency in mice lacking the c-abl gene.

Received for publication, May 12, 2006 , and in revised form, June 29, 2006.

^* 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 Figs. S1 and S2.

¹ To whom correspondence should be addressed. Tel.: 573-882-4593; Fax: 573-882-4287; E-mail: FangD{at}Missouri.edu.

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