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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
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
Citation
CANCER LETTERS Vol.314 No.2, pp. 198-205
Keywords
복합학TM4SF5Cytosolic p27Kip1JNKAdherence 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
URI
http://hdl.handle.net/10371/82069
DOI
https://doi.org/10.1016/j.canlet.2011.09.030
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College of Pharmacy (약학대학)Dept. of Pharmacy (약학과)Journal Papers (저널논문_약학과)
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