Binding of IFITM1 enhances the inhibiting effect of caveolin-1 on ERK activation
Binding of IFITM1 enhances the inhibiting effect of
caveolin-1 on ERK activation
Ye Xu;Guohua Yang;Gengxi Hu
【期刊名称】《生物化学与生物物理学报:英文版》 【年(卷),期】2009(041)006
【摘要】Interferon-induced transmembrane protein 1 (IFITM1)is an essential mediator of interferon-v-induced antiproliferation. Here, we reported the interaction between IFITM1 and caveolin-1 (CAV-1), and their inhibitory regulatory function on extracellular signal-regulated kinase (ERK). The immunofluorescence staining result showed that IFITM1 localized in caveolae of the plasma membrane and could interact with CAV-1. Deletion mutagenesis clearly revealed that the hydrophobic transmembrane domains were responsible for the interaction between IFITM1 and CAV-1. It has been reported that CAV-1 has inhibitory effect on the phosphorylation of ERK, and subsequently ERK-mediated transcription. Our study showed the interaction of IFITM1- and CAV-1-enbanced CAV-1's inhibitory effect on ERK activation, whereas the IFITM1 did not activate ERK directly. This inhibitory effect was further confirmed by knocking down the endogenous CAV-1 using RNA interference. These results revealed that the interaction between IFITM1 and CAV-1 could enhance the inhibitory effect of CAV-1 on ERK activation.
【总页数】7页(488-494) 【关键词】
【作者】Ye Xu;Guohua Yang;Gengxi Hu
【作者单位】State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences, Shanghai 200031, China;State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences, Shanghai 200031, China;State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences, Shanghai 200031, China
【正文语种】中文 【中图分类】Q5 【文献来源】
https://www.zhangqiaokeyan.com/academic-journal-cn_acta-biochimica-biophysica-sinica_thesis/0201254942892.html 【相关文献】
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