DC Field | Value | Language |
---|---|---|
dc.contributor.author | Choi, Myung-Suk | ko |
dc.contributor.author | Min, Sang-Hyun | ko |
dc.contributor.author | Jung, Haiyoung | ko |
dc.contributor.author | Lee, Ju Dong | ko |
dc.contributor.author | Lee, Tae Ho | ko |
dc.contributor.author | Lee, HeungKyu | ko |
dc.contributor.author | Yoo, Ook-Joon | ko |
dc.date.accessioned | 2013-03-12T04:53:21Z | - |
dc.date.available | 2013-03-12T04:53:21Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2011-03 | - |
dc.identifier.citation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.406, no.2, pp.305 - 309 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/10203/101369 | - |
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. (C) 2011 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | TYROSINE PHOSPHATASES | - |
dc.subject | COLORECTAL-CANCER | - |
dc.subject | DOWN-REGULATION | - |
dc.subject | METASTASIS | - |
dc.subject | EXPRESSION | - |
dc.subject | INVASION | - |
dc.subject | MOTILITY | - |
dc.subject | BCL-2 | - |
dc.subject | IDENTIFICATION | - |
dc.subject | PROGRESSION | - |
dc.title | The essential role of FKBP38 in regulating phosphatase of regenerating liver 3 (PRL-3) protein stability | - |
dc.type | Article | - |
dc.identifier.wosid | 000288616200026 | - |
dc.identifier.scopusid | 2-s2.0-79952443190 | - |
dc.type.rims | ART | - |
dc.citation.volume | 406 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 305 | - |
dc.citation.endingpage | 309 | - |
dc.citation.publicationname | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.contributor.localauthor | Lee, HeungKyu | - |
dc.contributor.localauthor | Yoo, Ook-Joon | - |
dc.contributor.nonIdAuthor | Choi, Myung-Suk | - |
dc.contributor.nonIdAuthor | Jung, Haiyoung | - |
dc.contributor.nonIdAuthor | Lee, Tae Ho | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | FKBP38 | - |
dc.subject.keywordAuthor | Phosphatase of regenerating liver 3 | - |
dc.subject.keywordAuthor | PRL-3 | - |
dc.subject.keywordAuthor | FK506-binding protein 38 | - |
dc.subject.keywordAuthor | Peptidyl prolyl cis/trans isomerase | - |
dc.subject.keywordPlus | TYROSINE PHOSPHATASES | - |
dc.subject.keywordPlus | COLORECTAL-CANCER | - |
dc.subject.keywordPlus | DOWN-REGULATION | - |
dc.subject.keywordPlus | METASTASIS | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | INVASION | - |
dc.subject.keywordPlus | MOTILITY | - |
dc.subject.keywordPlus | BCL-2 | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | PROGRESSION | - |
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