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

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dc.contributor.authorM S Choi-
dc.contributor.authorS H Min-
dc.contributor.authorHai Young Jung-
dc.contributor.authorJ D Lee-
dc.contributor.authorT H Lee-
dc.contributor.authorH K Lee-
dc.contributor.authorO J Yoo-
dc.date.accessioned2017-04-19T09:22:10Z-
dc.date.available2017-04-19T09:22:10Z-
dc.date.issued2011-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2011.02.037ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10045-
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.-
dc.publisherElsevier-
dc.titleThe essential role of FKBP38 in regulating phosphatase of regenerating liver 3(PRL-3) protein stability-
dc.title.alternativeThe essential role of FKBP38 in regulating phosphatase of regenerating liver 3(PRL-3) protein stability-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number2-
dc.citation.endPage309-
dc.citation.startPage305-
dc.citation.volume406-
dc.contributor.affiliatedAuthorHai Young Jung-
dc.contributor.alternativeName최명숙-
dc.contributor.alternativeName민상현-
dc.contributor.alternativeName정해용-
dc.contributor.alternativeName이주동-
dc.contributor.alternativeName이태호-
dc.contributor.alternativeName이흥규-
dc.contributor.alternativeName유욱준-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 406, no. 2, pp. 305-309-
dc.identifier.doi10.1016/j.bbrc.2011.02.037-
dc.subject.keywordFK506-binding protein 38-
dc.subject.keywordFKBP38-
dc.subject.keywordPeptidyl prolyl cis/trans isomerase-
dc.subject.keywordPhosphatase of regenerating liver 3-
dc.subject.keywordPRL-3-
dc.subject.localFK506-binding protein 38-
dc.subject.localFKBP38-
dc.subject.localpeptidyl-prolyl cis-trans isomerase-
dc.subject.localpeptidyl-prolyl cis/trans-isomerase-
dc.subject.localPeptidyl prolyl cis/trans isomerase-
dc.subject.localPhosphatase of regenerating liver 3-
dc.subject.localPhosphatase of regenerating liver-3-
dc.subject.localphosphatase of regenerating liver-3-
dc.subject.localPRL-3-
dc.description.journalClassY-
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Aging Convergence Research Center > 1. Journal Articles
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