| Maspin increases Ku70 acetylation and Bax-mediated cell death in cancer cells. | |
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MedLine Citation:
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PMID: 22076034 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Ku70, a DNA repair protein, was recently identified as a critical anti-apoptotic protein that inhibits Bax translocation to mitochondria. The dissociation of Bax from Ku70 is essential for the apoptotic activity of Bax. Here, we show that maspin, a tumor suppressor protein frequently lost in cancer, regulates this process. Maspin increased cell death in a Ku70 acetylation-dependent manner. Maspin inhibited histone deacetylase 1 (HDAC1) and thus increased the acetylation of Ku70 and the dissociation of Bax from Ku70, which led to the induction of apoptosis. These results reveal maspin as a Ku70-interacting molecule and provide the basis for a new endogenous acetylation-based control mechanism that reduces Ku70-mediated sequestration of Bax from mitochondria. |
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Authors:
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Sook-Ja Lee; Haerim Jang; Chaehwa Park |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-10 |
Journal Detail:
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Title: International journal of molecular medicine Volume: - ISSN: 1791-244X ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-14 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9810955 Medline TA: Int J Mol Med Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Cancer Genetics Laboratory, Biomedical Research Institute, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul 135-710, Republic of Korea. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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