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Acta Biochimica et Biophysica Sinica 2009 41(6):488-494; doi:10.1093/abbs/gmp034
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© The Author 2009. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

Binding of IFITM1 enhances the inhibiting effect of caveolin-1 on ERK activation

Ye Xu, Guohua Yang and Gengxi Hu*

State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China

* Correspondence address. Tel: +86-21-54921342; Fax: +86-21-54921011; E-mail: hgxgene{at}sunm.shcnc.ac.cn


  Abstract

Interferon-induced transmembrane protein 1 (IFITM1) is an essential mediator of interferon-{gamma}-induced anti-proliferation. 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-enhanced 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.

Keywords    interferon-induced transmembrane protein 1; caveolin-1; ERK; inhibitory effect

Received: December 2, 2008; Accepted: February 27, 2009
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