| Nuclear Akt interacts with B23/NPM and protects it from proteolytic cleavage, enhancing cell survival. | |
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MedLine Citation:
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PMID: 18931307 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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B23/NPM is a major nucleolar phosphoprotein that has a critical role in cell proliferation and cell death. Here, we show that it forms a complex with Akt on growth factor (GF) stimulation in both the cytoplasm and the nucleus, for which Akt activation is indispensable. The C terminus of B23 (239-294 residues) potently binds pleckstrin homology (PH) domain of Akt. Akt binding to B23 protects it from proteolytic degradation by caspase-3, leading to the up-regulation of cell survival. Interestingly, unsumoylated B23 K263R, but not wild-type B23, strongly interacts with Akt in the nucleoplasm in the absence of GFs. Furthermore, we show that Akt2, but not other isoforms, specifically regulates B23 sumoylation and protein stability. Also, nuclear Akt regulates the cell cycle progression activity of B23. Therefore, our findings support that nuclear Akt binds and stabilizes B23 in the nucleoplasm, and regulates its activities in cell survival and cell cycle. |
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Authors:
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Sang Bae Lee; Truong L Xuan Nguyen; Joung Woo Choi; Kyung-Hoon Lee; Sung-Woo Cho; Zhixue Liu; Keqiang Ye; Sun Sik Bae; Jee-Yin Ahn |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-10-17 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 105 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2008 Oct |
Date Detail:
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Created Date: 2008-10-29 Completed Date: 2008-12-01 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 16584-9 Citation Subset: IM |
Affiliation:
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Departments of Molecular Cell Biology and Anatomy and Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Binding Sites Caspase 3 / metabolism* Cell Cycle Cell Nucleus Cell Survival* Cytoplasm Hippocampus Nuclear Proteins / metabolism*, physiology PC12 Cells Proto-Oncogene Proteins c-akt / metabolism* Rats Ubiquitination |
| Grant Support | |
ID/Acronym/Agency:
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//Howard Hughes Medical Institute |
| Chemical | |
Reg. No./Substance:
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0/Nuclear Proteins; 117896-08-9/nucleophosmin; EC 2.7.1.37/Akt2 protein, rat; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 3.4.22.-/Caspase 3 |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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