| Literature DB >> 17728103 |
Heejae Tak1, Eunsun Jang, Seung Beom Kim, Jinhwi Park, Jinkyu Suk, Yoo Sik Yoon, Jeong Keun Ahn, Jeung-Hoon Lee, Cheol O Joe.
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.Entities:
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Year: 2007 PMID： 17728103 DOI： 10.1016/j.cellsig.2007.07.016
Source DB: PubMed Journal: Cell Signal ISSN： 0898-6568 Impact factor: 4.315