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- W2753865572 endingPage "170" @default.
- W2753865572 startingPage "165" @default.
- W2753865572 abstract "The Eya proteins were originally identified as essential transcriptional co-activators of the Six family of homeoproteins. Subsequently, the highly conserved C-terminal domains of the Eya proteins were discovered to act as a Mg2+-dependent Tyr phosphatases, making Eyas the first transcriptional activators to harbor intrinsic phosphatase activity. Only two direct targets of the Eya Tyr phosphatase have been identified: H2AX, whose dephosphorylation directs cells to the DNA repair instead of the apoptotic pathway upon DNA damage, and ERβ, whose dephosphorylation inhibits its anti-tumor transcriptional activity. The Eya Tyr phosphatase mediates breast cancer cell transformation, migration, invasion, as well as metastasis, through targets not yet identified. Intriguingly, the N-terminal domain of Eya contains a separate Ser/Thr phosphatase activity implicated in innate immunity and in regulating c-Myc stability. Thus, Eya proteins are highly complex, containing two separable phosphatase domains and a transcriptional activation domain, thereby influencing tumor progression through multiple mechanisms." @default.
- W2753865572 created "2017-09-15" @default.
- W2753865572 creator A5023441926 @default.
- W2753865572 creator A5041282060 @default.
- W2753865572 creator A5042493835 @default.
- W2753865572 creator A5050468415 @default.
- W2753865572 creator A5081927192 @default.
- W2753865572 date "2018-03-01" @default.
- W2753865572 modified "2023-10-15" @default.
- W2753865572 title "The Eya phosphatase: Its unique role in cancer" @default.
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