Publications

Detailed Information

JNK signaling activity regulates cell-cell adhesions via TM4SF5-mediated p27(Kip1) phosphorylation

Cited 12 time in Web of Science Cited 13 time in Scopus
Authors

Kim, Hyeonjung; Jung, Oisun; Kang, Minkyung; Lee, Mi-Sook; Jeong, Doyoung; Ryu, Jihye; Ko, Youra; Choi, Yoon-Ju; Lee, Jung Weon

Issue Date
2012-01
Publisher
Elsevier BV
Citation
Cancer Letters, Vol.314 No.2, pp.198-205
Abstract
Transmembrane 4 L six family member 5 (TM4SF5) can regulate cell-cell adhesion and cellular morphology via cytoplasmic p27(Kip1)-mediated changes in RhoA activity. However, how TM4SF5 causes cytosolic p27(Kip1) stabilization remains unknown. In this study we found that TM4SF5-mediated Ser10 phosphorylation of p27(Kip1) required for cytosolic localization was not always correlated with Akt activity. Inhibition or suppression of c-Jun N-terminal kinase (INK) in TM4SF5-expressing cells decreased Ser10 phosphorylation of p27(Kip1) and rescued expression levels and localization of adherence junction molecules to cell-cell contacts. These observations suggest involvement of JNKs in TM4SF5-mediated p27(Kip1) Ser10 phosphorylation and localization during epithelial-mesenchymal transition. (C) 2011 Elsevier Ireland Ltd. All rights reserved.
ISSN
0304-3835
Language
English
URI
https://hdl.handle.net/10371/82069
DOI
https://doi.org/10.1016/j.canlet.2011.09.030
Files in This Item:
There are no files associated with this item.
Appears in Collections:

Altmetrics

Item View & Download Count

  • mendeley

Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.

Share