14-3-3ε通过破坏F-肌动蛋白聚合来抑制MK5介导的细胞迁移。
14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin polymerization.
作者信息
Tak Heejae, Jang Eunsun, Kim Seung Beom, Park Jinhwi, Suk Jinkyu, Yoon Yoo Sik, Ahn Jeong Keun, Lee Jeung-Hoon, Joe Cheol O
机构信息
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, South Korea.
出版信息
Cell Signal. 2007 Nov;19(11):2379-87. doi: 10.1016/j.cellsig.2007.07.016. Epub 2007 Jul 31.
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.
在培养的HeLa细胞中研究了14-3-3ε抑制丝裂原活化蛋白激酶5（MK5）诱导的细胞迁移的信号通路。体内和体外分析均显示14-3-3ε与MK5相互作用。与MK5结合的14-3-3ε抑制了MK5的已知底物HSP27的磷酸化。在瞬时表达14-3-3ε的转染细胞以及稳定表达14-3-3ε的已建立细胞中均显示14-3-3ε会干扰肌动蛋白细胞骨架的组织。此外，14-3-3ε的过表达导致由MK5过表达或TNFα处理诱导的细胞迁移受到抑制。我们的结果表明，与MK5结合的14-3-3ε通过抑制HSP27的磷酸化来抑制细胞迁移，而HSP27的磷酸化调节F-肌动蛋白聚合、肌动蛋白细胞骨架组织以及随后的肌动蛋白丝动力学。
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