| SGT, a Hsp90beta binding partner, is accumulated in the nucleus during cell apoptosis. | |
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MedLine Citation:
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PMID: 16580629 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In this study, we reported that small glutamine-rich TPR-containing protein (SGT) interacted with not only Hsp90alpha but also Hsp90beta. Confocal analysis showed that treatment of cells with Hsp90-specific inhibitor geldanamycin (GA) disrupted the interaction of SGT with Hsp90beta and this contributed to the increase of nuclear localization of SGT in HeLa cells. The increased nuclear localization of SGT was further confirmed by the Western blotting in GA-treated HeLa cells and H1299 cells. In our previous study, SGT was found to be a new pro-apoptotic factor, so we wondered whether the sub-cellular localization of SGT was related with cell apoptosis. By confocal analysis we found that the nuclear import of SGT was significantly increased in STS-induced apoptotic HeLa cells, which implied that the sub-cellular localization of SGT was closely associated with Hsp90beta and apoptosis. |
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Authors:
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Hongyan Yin; Hanzhou Wang; Hongliang Zong; Xiaoning Chen; Yanlin Wang; Xiaojing Yun; Yihong Wu; Jiadong Wang; Jianxin Gu |
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Publication Detail:
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Type: Journal Article Date: 2006-03-24 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 343 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2006 May |
Date Detail:
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Created Date: 2006-04-26 Completed Date: 2006-06-09 Revised Date: 2007-05-30 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 1153-8 Citation Subset: IM |
Affiliation:
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Key Laboratory of Medical Molecular Virology Ministry of Education and Health, Gene Research Center, Shanghai Medical College and Institutes of Biomedical Sciences of Fudan University, Shanghai 200032, PR China. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Active Transport, Cell Nucleus Apoptosis* Carrier Proteins / biosynthesis, metabolism* Cell Line Cell Nucleus / metabolism* Cytoplasm / metabolism HSP90 Heat-Shock Proteins / antagonists & inhibitors, metabolism* Humans Protein Binding |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/HSP90 Heat-Shock Proteins; 0/HSP90AB1 protein, human; 0/SGTA protein, human |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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