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- W2162488397 endingPage "1897" @default.
- W2162488397 startingPage "1886" @default.
- W2162488397 abstract "Three classes of E3 ubiquitin ligases, members of the Cbl, Hakai, and SOCS-Cul5-RING ligase families, stimulate the ubiquitination of phosphotyrosine-containing proteins, including receptor and nonreceptor tyrosine kinases and their phosphorylated substrates. Because ubiquitination frequently routes proteins for degradation by the lysosome or proteasome, these E3 ligases are able to potently inhibit tyrosine kinase signaling. Their loss or mutational inactivation can contribute to cancer, autoimmunity, or endocrine disorders, such as diabetes. However, these ligases also have biological functions that are independent of their ubiquitination activity. Here we review relevant literature and then focus on more-recent developments in understanding the structures, substrates, and pathways through which the phosphotyrosine-specific ubiquitin ligases regulate diverse aspects of cell biology." @default.
- W2162488397 created "2016-06-24" @default.
- W2162488397 creator A5018410197 @default.
- W2162488397 creator A5024267978 @default.
- W2162488397 creator A5072832150 @default.
- W2162488397 date "2015-06-01" @default.
- W2162488397 modified "2023-10-16" @default.
- W2162488397 title "Cell Regulation by Phosphotyrosine-Targeted Ubiquitin Ligases" @default.
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