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Papers In Press, published online ahead of print April 11, 2003
J. Biol. Chem, 10.1074/jbc.M212887200
Submitted on December 18, 2002
Revised on April 10, 2003
Accepted on April 11, 2003

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

Biochemistry and Molecular Biology, Johns Hopkins University, Baltimore, MD 21205

Corresponding Author: cpickart{at}jhmi.edu

Ubiquitin-protein ligases (E3s) of the HECT family share a conserved catalytic region that is Homologous to the E6-AP Carboxyl 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 (TBP-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.


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