Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/4448
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dc.contributorDepartment of Health Technology and Informatics-
dc.creatorLin, CYen_US
dc.creatorTan, BCMen_US
dc.creatorLiu, Hen_US
dc.creatorShih, CJen_US
dc.creatorChien, KYen_US
dc.creatorLin, CLen_US
dc.creatorYung, BYMen_US
dc.date.accessioned2014-12-11T08:25:06Z-
dc.date.available2014-12-11T08:25:06Z-
dc.identifier.issn1059-1524en_US
dc.identifier.urihttp://hdl.handle.net/10397/4448-
dc.language.isoenen_US
dc.publisherThe American Society for Cell Biologyen_US
dc.rights© 2010 C. Y. Lin et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution– Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).en_US
dc.rightsThe following article appeared in Lin, C. Y. et al., Molecular Biology of the Cell, v. 21, no. 24, p. 4409-4417 and may be found at http://www.molbiolcell.org/content/21/24/4409.abstracten_US
dc.subjectCell lineen_US
dc.subjectDNA damageen_US
dc.subjectDNA repairen_US
dc.subjectDose-response relationship, radiationen_US
dc.subjectE2F1 transcription factor/geneticsen_US
dc.subjectE2F1 transcription factor/metabolismen_US
dc.subjectE2F1 transcription factor/physiologyen_US
dc.subjectGene expression regulation/radiation effectsen_US
dc.subjectMutation, missense/physiologyen_US
dc.subjectNuclear proteins/geneticsen_US
dc.subjectNuclear proteins/metabolismen_US
dc.subjectNuclear proteins/physiologyen_US
dc.subjectPhosphorylationen_US
dc.subjectProtein bindingen_US
dc.subjectProtein phosphatase 1/geneticsen_US
dc.subjectProtein phosphatase 1/metabolismen_US
dc.subjectProtein phosphatase 1/physiologyen_US
dc.subjectRetinoblastoma protein/geneticsen_US
dc.subjectRetinoblastoma protein/metabolismen_US
dc.subjectRetinoblastoma protein/physiologyen_US
dc.subjectTime factorsen_US
dc.subjectUltraviolet rays/adverse effectsen_US
dc.titleDephosphorylation of nucleophosmin by PP1β facilitates pRB binding and consequent E2F1-dependent DNA repairen_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.spage4409en_US
dc.identifier.epage4417en_US
dc.identifier.volume21en_US
dc.identifier.issue24en_US
dc.identifier.doi10.1091/mbc.E10-03-0239en_US
dcterms.abstractNucleophosmin (NPM) is an important phosphoprotein with pleiotropic functions in various cellular processes. Although phosphorylation has been postulated as an important functional determinant, possible regulatory roles of this modification on NPM are not fully characterized. Here, we find that NPM is dephosphorylated on various threonine residues (Thr199 and Thr234/237) in response to UV-induced DNA damage. Further experiments indicate that the serine/threonine protein phosphatase PP1β is a physiological NPM phosphatase under both the genotoxic stress and growth conditions. As a consequence, NPM in its hypophosphorylated state facilitates DNA repair. Finally, our results suggest that one possible mechanism of this protective response lies in enhanced NPM-retinoblastoma tumor suppressor protein (pRB) interaction, leading to the relief of the repressive pRB–E2F1 circuitry and the consequent transcriptional activation of E2F1 and several downstream DNA repair genes. Thus, this study unveils a key phosphatase of NPM and highlights a novel mechanism by which the PP1β–NPM pathway contributes to cellular DNA damage response.-
dcterms.accessRightsopen accessen_US
dcterms.bibliographicCitationMolecular Biology of the Cell, 15 Dec. 2010, v. 21, no. 24, p. 4409-4417en_US
dcterms.isPartOfMolecular Biology of the Cellen_US
dcterms.issued2010-12-15-
dc.identifier.isiWOS:000285343300011-
dc.identifier.scopus2-s2.0-78650487849-
dc.identifier.pmid20962268-
dc.identifier.rosgroupidr51160-
dc.description.ros2010-2011 > Academic research: refereed > Publication in refereed journal-
dc.description.oaVersion of Recorden_US
dc.identifier.FolderNumberOA_IR/PIRAen_US
dc.description.pubStatusPublisheden_US
dc.description.oaCategoryCCen_US
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