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J. Biol. Chem., Vol. 278, Issue 26, 23369-23375, June 27, 2003

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Proteolytic Targeting of Transcriptional Regulator TIP120B by a HECT Domain E3 Ligase^*

Jianxin You  , Min Wang , Tsutomu Aoki ¶ ||, Taka-aki Tamura ¶ and Cecile M. Pickart  **

From the Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205 and ^¶Department of Biology, Faculty of Science, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan

Ubiquitin-protein ligases (E3s) of the HECT family share a conserved catalytic region that is homologous to the E6-AP C terminus. The HECT domain defines a large E3 family, but only a handful of these enzymes have been defined with respect to substrate specificity or biological function. We showed previously that the C-terminal domain of one family member, KIAA10, catalyzes the assembly of polyubiquitin chains, whereas the N-terminal domain binds to proteasomes in vitro (You, J., and Pickart, C. M. (2001) J. Biol. Chem. 276, 19871–19878). We show here that KIAA10 also associates with proteasomes within cells but that this association probably involves additional contacts with proteasome subunits other than the one (S2/Rpn1) identified in our previous work. We report that the N-domain of KIAA10 also mediates an association with TIP120B (TATA-binding protein-interacting protein 120B), a putative transcriptional regulator. Biochemical and co-transfection studies revealed that TIP120B, but not the closely related protein TIP120A, is a specific substrate of KIAA10 in vitro and within C2C12 myoblasts but not in Cos-1 cells. KIAA10 and TIP120B are both highly expressed in human skeletal muscle, suggesting that KIAA10 may regulate TIP120B homeostasis specifically in this tissue.

Received for publication, December 18, 2002 , and in revised form, April 10, 2003.

^* This work was supported by National Institutes of Health Grant DK46984. 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.

Current addresses: Dept. of Pathology, Harvard Medical School, Boston, MA 02115.

^|| Dept. of Molecular Biology, Princeton University, Princeton, NJ 08544.

^** To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Johns Hopkins University, 615 North Wolfe St., Baltimore, MD 21205. Tel.: 410-614-4554; Fax: 410-955-2926; E-mail: cpickart{at}jhmi.edu.

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