The study demonstrates that IFITM1 interacts with CAV-1 to enhance its inhibitory effect on ERK activation, providing insights into the molecular mechanisms of interferon-gamma-induced antiproliferation.
Hypothesis-generating for IFITM1-CAV-1 modulation of ERK in antiproliferative signaling; leaves open translation to human cardiovascular disease.
Interferon-induced transmembrane protein 1 (IFITM1) is an essential mediator of interferon-g-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-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.
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Xu et al. (2009) studied this question.
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