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

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Title
The essential role of FKBP38 in regulating phosphatase of regenerating liver 3(PRL-3) protein stability
Author(s)
M S Choi; S H Min; Hai Young Jung; J D Lee; T H Lee; H K Lee; O J Yoo
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 406, no. 2, pp. 305-309
Publication Year
2011
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.
Keyword
FK506-binding protein 38FKBP38Peptidyl prolyl cis/trans isomerasePhosphatase of regenerating liver 3PRL-3
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2011.02.037
Type
Article
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
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