کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1964304 | 1058540 | 2007 | 9 صفحه PDF | دانلود رایگان |
The signal pathway by which 14-3-3ɛ 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 14-3-3ɛ interacts with MK5. 14-3-3ɛ bound to MK5 inhibits the phosphorylation of HSP27, a known substrate of MK5. Disturbance of actin cytoskeleton organization by 14-3-3ɛ was shown in transfected cells transiently expressing 14-3-3ɛ as well as established cells stably expressing 14-3-3ɛ. Moreover, overexpression of 14-3-3ɛ resulted in the inhibition of cell migration induced by MK5 overexpression or TNFα treatment. Our results suggest that 14-3-3ɛ 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.
Journal: Cellular Signalling - Volume 19, Issue 11, November 2007, Pages 2379–2387