| hPuf-A/KIAA0020 Modulates PARP-1 Cleavage upon Genotoxic Stress. | |
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MedLine Citation:
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PMID: 21266351 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Human hPuf-A/KIAA0020 was first identified as a new minor histocompatibility antigen in 2001. Its zebrafish orthologue contains six Pumilio-homology RNA-binding domains and has been shown to participate in the development of eyes and primordial germ cells, but the cellular function of hPuf-A remains unclear. In this report, we showed that hPuf-A predominantly localized in the nucleoli with minor punctate signals in the nucleoplasm. The nucleolar localization of hPuf-A would redistribute to the nucleoplasm after the treatment of RNA polymerase inhibitors (actinomycin D and 5,6-dichlorobenzimidazole riboside) and topoisomerase inhibitors [camptothecin (CPT) and etoposide]. Interestingly, knockdown of hPuf-A sensitized cells to CPT and UV treatment and cells constitutively overexpressing hPuf-A became more resistant to genotoxic exposure. Affinity gel pull-down coupled with mass spectrometric analysis identified PARP-1 as one of the hPuf-A interacting proteins. hPuf-A specifically interacts with the catalytic domain of PARP-1 and inhibits poly(ADP-ribosyl)ation of PARP-1 in vitro. Depletion of hPuf-A increased the cleaved PARP-1 and overexpression of hPuf-A lessened PARP-1 cleavage when cells were exposed to CPT and UV light. Collectively, hPuf-A may regulate cellular response to genotoxic stress by inhibiting PARP-1 activity and thus preventing PARP-1 degradation by caspase-3. Cancer Res; 71(3); 1126-34. ©2011 AACR. |
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Authors:
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Hao-Yen Chang; Chi-Chen Fan; Po-Chen Chu; Bo-En Hong; Hyeon Jeong Lee; Mau-Sun Chang |
Publication Detail:
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Type: Journal Article Date: 2011-01-25 |
Journal Detail:
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Title: Cancer research Volume: 71 ISSN: 1538-7445 ISO Abbreviation: Cancer Res. Publication Date: 2011 Feb |
Date Detail:
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Created Date: 2011-02-02 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2984705R Medline TA: Cancer Res Country: United States |
Other Details:
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Languages: eng Pagination: 1126-34 Citation Subset: IM |
Affiliation:
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Authors' Affiliations: Institute of Biochemical Sciences, College of Life Science, National Taiwan University; Department of Physiology, Mackay Memorial Hospital; Department of Biochemical Science and Technology, College of Life Science, National Taiwan University; and Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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