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- W17382811 endingPage "306" @default.
- W17382811 startingPage "253" @default.
- W17382811 abstract "Tyrosine phosphorylation of proteins serves as an exquisite switch in controlling several key oncogenic signaling pathways involved in cell proliferation, apoptosis, migration, and invasion. Since protein tyrosine phosphatases (PTPs) counteract protein kinases by removing phosphate moieties on target proteins, one may intuitively think that PTPs would act as tumor suppressors. Indeed, one of the most described PTPs, namely, the phosphatase and tensin homolog (PTEN), is a tumor suppressor. However, a growing body of evidence suggests that PTPs can also function as potent oncoproteins. In this chapter, we provide a broad historical overview of the PTPs, their mechanism of action, and posttranslational modifications. Then, we focus on the dual properties of classical PTPs (receptor and nonreceptor) and dual-specificity phosphatases in cancer and summarize the current knowledge of the signaling pathways regulated by key PTPs in human cancer. In conclusion, we present our perspective on the potential of these PTPs to serve as therapeutic targets in cancer." @default.
- W17382811 created "2016-06-24" @default.
- W17382811 creator A5007653418 @default.
- W17382811 creator A5017989928 @default.
- W17382811 creator A5073985215 @default.
- W17382811 date "2012-01-01" @default.
- W17382811 modified "2023-10-14" @default.
- W17382811 title "Protein Tyrosine Phosphatases in Cancer" @default.
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