The essential role of FKBP38 in regulating phosphatase of regenerating liver 3 (PRL-3) protein stability

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dc.contributor.authorChoi, Myung-Sukko
dc.contributor.authorMin, Sang-Hyunko
dc.contributor.authorJung, Haiyoungko
dc.contributor.authorLee, Ju Dongko
dc.contributor.authorLee, Tae Hoko
dc.contributor.authorLee, HeungKyuko
dc.contributor.authorYoo, Ook-Joonko
dc.date.accessioned2013-03-12T04:53:21Z-
dc.date.available2013-03-12T04:53:21Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2011-03-
dc.identifier.citationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.406, no.2, pp.305 - 309-
dc.identifier.issn0006-291X-
dc.identifier.urihttp://hdl.handle.net/10203/101369-
dc.description.abstractThe phosphatase of regenerating liver-3 (PRL-3) is a member of protein tyrosine phosphatases and whose deregulation is implicated in tumorigenesis and metastasis of many cancers. However, the underlying mechanism by which PRL-3 is regulated is not known. In this study, we identified the peptidyl prolyl cis/trans isomerase FK506-binding protein 38 (FKBP38) as an interacting protein of PRL-3 using a yeast two-hybrid system. FKBP38 specifically binds to PRL-3 in vivo, and that the N-terminal region of FKBP38 is crucial for binding with PRL-3. FKBP38 overexpression reduces endogenous PRL-3 expression levels, whereas the depletion of FKBP38 by siRNA increases the level of PRL-3 protein. Moreover, FKBP38 promotes degradation of endogenous PRL-3 protein via protein-proteasome pathway. Furthermore, FKBP38 suppresses PRL-3-mediated p53 activity and cell proliferation. These results demonstrate that FKBP38 is a novel regulator of the oncogenic protein PRL-3 abundance and that alteration in the stability of PRL-3 can have a dramatic impact on cell proliferation. Thus, FKBP38 may play a critical role in tumorigenesis. (C) 2011 Elsevier Inc. All rights reserved.-
dc.languageEnglish-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.subjectTYROSINE PHOSPHATASES-
dc.subjectCOLORECTAL-CANCER-
dc.subjectDOWN-REGULATION-
dc.subjectMETASTASIS-
dc.subjectEXPRESSION-
dc.subjectINVASION-
dc.subjectMOTILITY-
dc.subjectBCL-2-
dc.subjectIDENTIFICATION-
dc.subjectPROGRESSION-
dc.titleThe essential role of FKBP38 in regulating phosphatase of regenerating liver 3 (PRL-3) protein stability-
dc.typeArticle-
dc.identifier.wosid000288616200026-
dc.identifier.scopusid2-s2.0-79952443190-
dc.type.rimsART-
dc.citation.volume406-
dc.citation.issue2-
dc.citation.beginningpage305-
dc.citation.endingpage309-
dc.citation.publicationnameBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.contributor.localauthorLee, HeungKyu-
dc.contributor.localauthorYoo, Ook-Joon-
dc.contributor.nonIdAuthorChoi, Myung-Suk-
dc.contributor.nonIdAuthorJung, Haiyoung-
dc.contributor.nonIdAuthorLee, Tae Ho-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorFKBP38-
dc.subject.keywordAuthorPhosphatase of regenerating liver 3-
dc.subject.keywordAuthorPRL-3-
dc.subject.keywordAuthorFK506-binding protein 38-
dc.subject.keywordAuthorPeptidyl prolyl cis/trans isomerase-
dc.subject.keywordPlusTYROSINE PHOSPHATASES-
dc.subject.keywordPlusCOLORECTAL-CANCER-
dc.subject.keywordPlusDOWN-REGULATION-
dc.subject.keywordPlusMETASTASIS-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusINVASION-
dc.subject.keywordPlusMOTILITY-
dc.subject.keywordPlusBCL-2-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusPROGRESSION-
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