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Molecular and Cellular Biology, February 2006, p. 1386-1397, Vol. 26, No. 4
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.4.1386-1397.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of SAP25, a Novel Component of the mSin3 Corepressor Complex

Yuzuru Shiio,1,2,3 David W. Rose,4 Radin Aur,4 Sam Donohoe,2 Ruedi Aebersold,2,5 and Robert N. Eisenman1*

Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109-1024,1 Institute for Systems Biology, Seattle, Washington 98103-8904,2 Children's Cancer Research Institute, The University of Texas Health Science Center, San Antonio, Texas 78229-3900,3 Department of Medicine and Cancer Center, University of California at San Diego, San Diego, California 92093-0673,4 Institute for Molecular Systems Biology, ETH-Zurich, and Faculty of Natural Sciences, University of Zurich, Zurich, Switzerland5

Received 5 July 2005/ Returned for modification 25 July 2005/ Accepted 25 November 2005

The transcriptional corepressor mSin3 is associated with histone deacetylases (HDACs) and is utilized by many DNA-binding transcriptional repressors. We have cloned and characterized a novel mSin3A-binding protein, SAP25. SAP25 binds to the PAH1 domain of mSin3A, associates with the mSin3A-HDAC complex in vivo, and represses transcription when tethered to DNA. SAP25 is required for mSin3A-mediated, but not N-CoR-mediated, repression. SAP25 is a nucleocytoplasmic shuttling protein, actively exported from the nucleus by a CRM1-dependent mechanism. A fraction of SAP25 is located in promyelocytic leukemia protein (PML) nuclear bodies, and PML induces a striking nuclear accumulation of SAP25. An isotope-coded affinity tag quantitative proteomic analysis of the SAP25 complex revealed that SAP25 is associated with several components of the mSin3 complex, nuclear export machinery, and regulators of transcription and cell cycle. These results suggest that SAP25 is a novel core component of the mSin3 corepressor complex whose subcellular location is regulated by PML.

* Corresponding author. Mailing address: Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109-1024. Phone: (206) 667-4445. Fax: (206) 667-6522. E-mail: eisenman{at}fhcrc.org.

Molecular and Cellular Biology, February 2006, p. 1386-1397, Vol. 26, No. 4
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.4.1386-1397.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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