JNK signaling activity regulates cell-cell adhesions via TM4SF5-mediated p27Kip1 phosphorylation
- Kim, Hyeonjung; Jung, Oisun; Kang, Minkyung; Lee, Mi-Sook; Jeong, Doyoung; Ryu, Jihye; Ko, Youra; Choi, Yoon-Ju; Lee, Jung Weon
- Issue Date
- CANCER LETTERS Vol.314 No.2, pp. 198-205
- 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.
- Files in This Item: There are no files associated with this item.