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JNK signaling activity regulates cell-cell adhesions via TM4SF5-mediated p27Kip1 phosphorylation
Cited 11 time in
Web of Science
Cited 12 time in Scopus
- Authors
- Issue Date
- 2012-01
- Publisher
- ELSEVIER
- Citation
- CANCER LETTERS Vol.314 No.2, pp. 198-205
- Keywords
- 복합학 ; TM4SF5 ; Cytosolic p27Kip1 ; JNK ; Adherence junction
- Abstract
- Transmembrane 4 L six family member 5 (TM4SF5) can regulate cell–cell adhesion and cellular
morphology via cytoplasmic p27Kip1-mediated changes in RhoA activity. However,
how TM4SF5 causes cytosolic p27Kip1 stabilization remains unknown. In this study we
found that TM4SF5-mediated Ser10 phosphorylation of p27Kip1 required for cytosolic localization
was not always correlated with Akt activity. Inhibition or suppression of c-Jun Nterminal
kinase (JNK) in TM4SF5-expressing cells decreased Ser10 phosphorylation of
p27Kip1 and rescued expression levels and localization of adherence junction molecules
to cell–cell contacts. These observations suggest involvement of JNKs in TM4SF5-mediated
p27Kip1 Ser10 phosphorylation and localization during epithelial–mesenchymal transition.
- ISSN
- 0304-3835
- Language
- English
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