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- W2155773951 abstract "E6-associated protein (E6AP) is a cellular ubiquitin protein ligase that mediates ubiquitylation and degradation of p53 in conjunction with the high-risk human papillomavirus E6 proteins. However, the physiological functions of E6AP are poorly understood. To identify a novel biological function of E6AP, we screened for binding partners of E6AP using GST pull-down and mass spectrometry. Here we identified annexin A1, a member of the annexin superfamily, as an E6AP-binding protein. Ectopic expression of E6AP enhanced the degradation of annexin A1 in vivo. RNAi-mediated downregulation of endogenous E6AP increased the levels of endogenous annexin A1 protein. E6AP interacted with annexin A1 and induced its ubiquitylation in a Ca2+-dependent manner. GST pull-down assay revealed that the annexin repeat domain III of annexin A1 is important for the E6AP binding. Taken together, our data suggest that annexin A1 is a novel substrate for E6AP-mediated ubiquitylation. Our findings raise the possibility that E6AP may play a role in controlling the diverse functions of annexin A1 through the ubiquitin-proteasome pathway. J. Cell. Biochem. 106: 1123–1135, 2009. © 2009 Wiley-Liss, Inc." @default.
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- W2155773951 date "2009-04-15" @default.
- W2155773951 modified "2023-09-27" @default.
- W2155773951 title "Identification of annexin A1 as a novel substrate for E6AP-mediated ubiquitylation" @default.
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- W2155773951 doi "https://doi.org/10.1002/jcb.22096" @default.
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