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- W2980402008 abstract "The protein composition of the plasma membrane is rapidly remodeled in response to changes in nutrient availability or cellular stress. This occurs, in part, through the selective ubiquitylation and endocytosis of plasma membrane proteins, which in the yeast Saccharomyces cerevisiae is mediated by the HECT E3 ubiquitin ligase Rsp5 and arrestin--related trafficking (ART) adaptors. Here, we provide evidence that the ART protein family members are composed of an arrestin fold with interspersed disordered loops. Using Art1 as a model, we show that these loop and tail regions, while not strictly required for function, regulate its activity through two separate mechanisms. Disruption of one loop mediates Art1 substrate specificity. Other loops are subjected to phosphorylation in a manner dependent on the Pho85 cyclins Clg1 and Pho80. Phosphorylation of the loops controls Art1's localization to the plasma membrane, which promotes cargo ubiquitylation and endocytosis, demonstrating a mechanism through which Art1 activity is regulated." @default.
- W2980402008 created "2019-10-25" @default.
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- W2980402008 creator A5051960969 @default.
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- W2980402008 creator A5087520347 @default.
- W2980402008 date "2019-12-01" @default.
- W2980402008 modified "2023-10-01" @default.
- W2980402008 title "Activity of a ubiquitin ligase adaptor is regulated by disordered insertions in its arrestin domain" @default.
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- W2980402008 doi "https://doi.org/10.1091/mbc.e19-08-0451" @default.
- W2980402008 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6880881" @default.
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