Title of article :
JNK signaling activity regulates cell–cell adhesions via TM4SF5-mediated p27Kip1 phosphorylation
Author/Authors :
Kim، نويسنده , , Hyeonjung and Jung، نويسنده , , Oisun and Kang، نويسنده , , Minkyung and Lee، نويسنده , , Mi-Sook and Jeong، نويسنده , , Doyoung and Ryu، نويسنده , , Jihye and Ko، نويسنده , , Youra and Choi، نويسنده , , Yoon-Ju and Lee، نويسنده , , Jung Weon Lee، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2012
Pages :
8
From page :
198
To page :
205
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 N-terminal 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.
Keywords :
TM4SF5 , JNK , Adherence junction , Cytosolic p27Kip1
Journal title :
Cancer Letters
Serial Year :
2012
Journal title :
Cancer Letters
Record number :
1820829
Link To Document :
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