PHLPP1 regulates contact inhibition by dephosphorylating Mst1 at the inhibitory site

Cited 6 time in scopus
Metadata Downloads
Title
PHLPP1 regulates contact inhibition by dephosphorylating Mst1 at the inhibitory site
Author(s)
S Jung; Jeong Gu Kang; Ju Hee Lee; Kyoung Jin Song; Jeong Heon KoYong Sam Kim
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 443, no. 4, pp. 1263-1269
Publication Year
2014
Abstract
Contact inhibition has been largely elusive despite that a loss of contact inhibition is a critical event for cancer development and progression. Here, we report that PHLPP1 is a binding protein for Mst1 and it modulates the Hippo pathway by dephosphorylating Mst1 at the inhibitory Thr387 of Mst1. Yap1 was localized predominantly in the nucleus but marginally in the cytoplasm in HeLa cells under sparse conditions, whereas the functional protein was more directed to sequestration in the cytoplasm under dense environments. Furthermore, loss of PHLPP1 resulted in a failure of the apoptotic control. It is interesting that down-regulated expression of PHLPP1 appears to mimic the loss of contact inhibition, a hallmark of cancer.
Keyword
Contact inhibitionHippo pathwayMst1PHLPP1
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2013.12.129
Type
Article
Appears in Collections:
Division of Biomedical Research > Genome Editing Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.