DC Field | Value | Language |
---|---|---|
dc.contributor.author | M S Choi | - |
dc.contributor.author | S H Min | - |
dc.contributor.author | Hai Young Jung | - |
dc.contributor.author | J D Lee | - |
dc.contributor.author | T H Lee | - |
dc.contributor.author | H K Lee | - |
dc.contributor.author | O J Yoo | - |
dc.date.accessioned | 2017-04-19T09:22:10Z | - |
dc.date.available | 2017-04-19T09:22:10Z | - |
dc.date.issued | 2011 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | 10.1016/j.bbrc.2011.02.037 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/10045 | - |
dc.description.abstract | The 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.publisher | Elsevier | - |
dc.title | The essential role of FKBP38 in regulating phosphatase of regenerating liver 3(PRL-3) protein stability | - |
dc.title.alternative | The essential role of FKBP38 in regulating phosphatase of regenerating liver 3(PRL-3) protein stability | - |
dc.type | Article | - |
dc.citation.title | Biochemical and Biophysical Research Communications | - |
dc.citation.number | 2 | - |
dc.citation.endPage | 309 | - |
dc.citation.startPage | 305 | - |
dc.citation.volume | 406 | - |
dc.contributor.affiliatedAuthor | Hai Young Jung | - |
dc.contributor.alternativeName | 최명숙 | - |
dc.contributor.alternativeName | 민상현 | - |
dc.contributor.alternativeName | 정해용 | - |
dc.contributor.alternativeName | 이주동 | - |
dc.contributor.alternativeName | 이태호 | - |
dc.contributor.alternativeName | 이흥규 | - |
dc.contributor.alternativeName | 유욱준 | - |
dc.identifier.bibliographicCitation | Biochemical and Biophysical Research Communications, vol. 406, no. 2, pp. 305-309 | - |
dc.identifier.doi | 10.1016/j.bbrc.2011.02.037 | - |
dc.subject.keyword | FK506-binding protein 38 | - |
dc.subject.keyword | FKBP38 | - |
dc.subject.keyword | Peptidyl prolyl cis/trans isomerase | - |
dc.subject.keyword | Phosphatase of regenerating liver 3 | - |
dc.subject.keyword | PRL-3 | - |
dc.subject.local | FK506-binding protein 38 | - |
dc.subject.local | FKBP38 | - |
dc.subject.local | peptidyl-prolyl cis-trans isomerase | - |
dc.subject.local | peptidyl-prolyl cis/trans-isomerase | - |
dc.subject.local | Peptidyl prolyl cis/trans isomerase | - |
dc.subject.local | Phosphatase of regenerating liver 3 | - |
dc.subject.local | Phosphatase of regenerating liver-3 | - |
dc.subject.local | phosphatase of regenerating liver-3 | - |
dc.subject.local | PRL-3 | - |
dc.description.journalClass | Y | - |
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