14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin polymerization

  • Cell Signal. 2007 Nov;19(11):2379-87. doi: 10.1016/j.cellsig.2007.07.016.
Heejae Tak  1 ,  Eunsun Jang ,  Seung Beom Kim ,  Jinhwi Park ,  Jinkyu Suk ,  Yoo Sik Yoon ,  Jeong Keun Ahn ,  Jeung-Hoon Lee ,  Cheol O Joe
Affiliations
  • 1. Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, South Korea.
PMID: 17728103 DOI: 10.1016/j.cellsig.2007.07.016
Abstract

The signal pathway by which 14-3-3epsilon inhibits cell migration induced by MAPK-activated protein kinase 5 (MK5) was investigated in cultured HeLa cells. Both in vivo and in vitro analyses have revealed that 14-3-3epsilon interacts with MK5. 14-3-3epsilon bound to MK5 inhibits the phosphorylation of HSP27, a known substrate of MK5. Disturbance of actin Cytoskeleton organization by 14-3-3epsilon was shown in transfected cells transiently expressing 14-3-3epsilon as well as established cells stably expressing 14-3-3epsilon. Moreover, overexpression of 14-3-3epsilon resulted in the inhibition of cell migration induced by MK5 overexpression or TNFalpha treatment. Our results suggest that 14-3-3epsilon bound to MK5 inhibits cell migration by inhibiting the phosphorylation of HSP27 whose phosphorylation regulates F-actin polymerization, actin Cytoskeleton organization and subsequent actinfilament dynamics.