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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
- 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
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