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Originally published In Press as doi:10.1074/jbc.M212988200 on March 26, 2003
J. Biol. Chem., Vol. 278, Issue 22, 20059-20068, May 30, 2003
SAFB2, a New Scaffold Attachment Factor Homolog and Estrogen Receptor Corepressor*
Steven M. Townson ,
Klaudia M. Dobrzycka ,
Adrian V. Lee ,
Mamie Air ,
Wanleng Deng ,
Kaiyan Kang ,
Shiming Jiang ,
Noriyuki Kioka ¶,
Kai Michaelis || and
Steffi Oesterreich **
From the
Breast Center, Department of Medicine, and Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030 adn the ¶Laboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University, Kyoto 606-8502, Japan
We have characterized previously the nuclear matrix protein/scaffold attachment factor (SAFB) as an estrogen receptor corepressor and as a potential tumor suppressor gene in breast cancer. A search of the human genome for other potential SAFB family members revealed that KIAA00138 (now designated as SAFB2) has high homology to SAFB (now designated as SAFB1). SAFB1 and SAFB2 are mapped adjacent to each other on chromosome 19p13.3 and are arranged in a bidirectional divergent configuration (head to head), being separated by a short (<500 bp) GC-rich intergenic region that can function as a bidirectional promoter. SAFB1 and SAFB2 share common functions but also have unique properties. As shown previously for SAFB1, SAFB2 functions as an estrogen receptor corepressor, and its overexpression results in inhibition of proliferation. SAFB1 and SAFB2 interact directly through a C-terminal domain, resulting in additive repression activity. They are coexpressed in a number of tissues, but unlike SAFB1, which is exclusively nuclear, SAFB2 is found in the cytoplasm as well as the nucleus. Consistent with its cytoplasmic localization, we detected an interaction between SAFB2 and vinexin, a protein involved in linking signaling to the cytoskeleton. Our findings suggest that evolutionary duplication of the SAFB gene has allowed it to retain crucial functions, but also to gain novel functions in the cytoplasm and/or nucleus.
Received for publication, December 19, 2002
, and in revised form, March 6, 2003.
* This work was supported in part by National Institutes of Health Grants K01 CA-77674 and R01 CA-97213 (to S. O.). 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.
Supported by United States Army Medical Research Material Command Grant DAMD-17-01-1-0146.
|| Present address: Institut für Molekulare Infektionsbiologie, Universität Würzburg, Röntgenring 11, Würzburg, Germany.
** To whom correspondence should be addressed: Breast Center, Baylor College of Medicine, One Baylor Plaza, BCM 600, Houston, TX 77030. Tel.: 713-798-1623; Fax: 713-798-1642; E-mail: steffio{at}breastcenter.tmc.edu.

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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