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Originally published In Press as doi:10.1074/jbc.M301157200 on April 9, 2003 Originally published In Press as doi:10.1074/jbc.M301157200 on April 1, 2003

J. Biol. Chem., Vol. 278, Issue 24, 21930-21937, June 13, 2003
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The BAL-binding Protein BBAP and Related Deltex Family Members Exhibit Ubiquitin-Protein Isopeptide Ligase Activity*

Kunihiko Takeyama {ddagger}, Ricardo C. T. Aguiar {ddagger}, Liqun Gu {ddagger}, Chunyan He {ddagger}, Gordon J. Freeman {ddagger}, Jeffery L. Kutok §, Jon C. Aster § and Margaret A. Shipp {ddagger} ¶

From the {ddagger} Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, § Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115

Members of the DTX (Deltex) family act as Notch signaling modifiers and may also regulate transcription through interactions with specific transcription factors. DTX proteins have a basic N terminus; a central proline-rich region; and a C-terminal RING finger domain, a motif often found in ubiquitin-protein isopeptide ligases (E3). Recently, we identified and characterized a unique diffuse large B-cell lymphoma risk-related gene named BAL (B aggressive lymphoma). Using a yeast two-hybrid screen for BAL-binding partners, we have now identified a novel protein termed BBAP (B-lymphoma- and BAL-associated protein). Although BBAP has a unique N terminus, the C-terminal region is highly homologous to that of DTX family members. Herein, we report that BBAP and the human family of DTX proteins (DTX1, DTX2, and DTX3) function as E3 ligases based on their capacity for self-ubiquitination. DTX family members homodimerize and heterodimerize in vivo, suggesting that physical interactions between various DTX family members modify E3 activity and/or substrate availability. Consistent with this idea, BBAP and DTX1 associate via their unique N termini, resulting in enhanced self-ubiquitination.

Received for publication, February 3, 2003 , and in revised form, March 24, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY225123, AY225124, AY225125, and AY225126.

* This work was supported by a Lymphoma Research Foundation fellowship (to K. T.), the Leukemia and Lymphoma Society of America (6624-01 to M. A. S. and 3093-00 to R. C. T. A.), and the V Foundation (to R. C. T. A.). 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.

To whom correspondence should be addressed: Dept. of Medical Oncology, Dana-Farber Cancer Inst., 44 Binney St., Boston, MA 02115. Tel.: 617-632-3874; Fax: 617-632-4734; E-mail: margaret_shipp{at}dfci.harvard.edu.


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