Genetic alterations of protein tyrosine phosphatases in human cancers

Zhao, Shuliang; Sedwick, David; Wang, Zhenghe

doi:10.1038/onc.2014.326

Cited by 64 publications

(60 citation statements)

References 124 publications

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“…Consistent with previous studies [38,39], PTPRT was mutated in 17% of all metastatic lung cancer samples, while PTPRD and PTPRS were mutated in 18% and 7% of the samples respectively. At least one of these PTPRs was mutated in 33% of all samples ( Table 1).…”

Section: Mutations In Protein Receptor Tyrosine Phosphatases and Statsupporting

confidence: 78%

Identification of Subsets of Genetic Alterations in KRAS-mutant Lung Cancer using Association Rule Mining

Tayou¹

2017

Preprint

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Section: Mutations In Protein Receptor Tyrosine Phosphatases and Statsupporting

confidence: 78%

Identification of Subsets of Genetic Alterations in KRAS-mutant Lung Cancer using Association Rule Mining

Tayou¹

2017

Preprint

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“…These cascade events and the finely-tuned regulation of kinases have been recognized as the core of signaling pathways. Specifically, phosphorylation of tyrosine residues in proteins has been intimately associated with the etiology of many human diseases, such as cancer (1)(2)(3).…”

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confidence: 99%

Defining the Protein-Protein Interaction Network of the Human Protein Tyrosine Phosphatase Family

Tran

Aziz

et al. 2016

Molecular & Cellular Proteomics

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Protein tyrosine phosphorylation, which plays a vital role in a variety of human cellular processes, is coordinated by protein tyrosine kinases and protein tyrosine phosphatases (PTPs). Genomic studies provide compelling evidence that PTPs are frequently mutated in various human cancers, suggesting that they have important roles in tumor suppression. However, the cellular functions and regulatory machineries of most PTPs are still largely unknown. To gain a comprehensive understanding of the protein-protein interaction network of the human PTP family, we performed a global proteomic study. Using a Minkowski distance-based unified scoring environment (MUSE) for the data analysis, we identified 940 high confidence candidate-interacting proteins that comprise the interaction landscape of the human PTP family. Through a gene ontology analysis and functional validations, we connected the PTP family with several key signaling pathways or cellular functions whose associations were previously unclear, such as the RAS-RAF-MEK pathway, the Hippo-YAP pathway, and cytokinesis. Our study provides the first glimpse of a protein interaction network for the human PTP family, linking it to a number of crucial signaling events, and generating a useful resource for future studies of PTPs. Molecular & Cellular Proteomics 15: 10.1074/mcp.M116.060277, 3030-3044, 2016.

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“…Somatic mutations in the PTP gene superfamily are found in different tumor types, with PTPRP being the most frequently mutated PTP in human cancer (Zhao et al, 2015). PTP, nonreceptor type 11 (PTPN11, also known as SHP2), was the first bona fide tyrosine phosphatase to be identified as an oncogene (Tartaglia et al, 2003;Loh et al, 2004, Mohi et al, 2005.…”

Section: Introductionmentioning

confidence: 99%

463 PTPN11 is a central node in intrinsic and acquired resistance to targeted cancer drugs

Prahallad¹

2014

European Journal of Cancer

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SUMMARYMost BRAF (V600E) mutant melanomas are sensitive to selective BRAF inhibitors, but BRAF mutant colon cancers are intrinsically resistant to these drugs because of feedback activation of EGFR.We performed an RNA-interference-based genetic screen in BRAF mutant colon cancer cells to search for phosphatases whose knockdown induces sensitivity to BRAF inhibition. We found that suppression of protein tyrosine phosphatase non-receptor type 11 (PTPN11) confers sensitivity to BRAF inhibitors in colon cancer. Mechanistically, we found that inhibition of PTPN11 blocks signaling from receptor tyrosine kinases (RTKs) to the RAS-MEK-ERK pathway. PTPN11 suppression is lethal to cells that are driven by activated RTKs and prevents acquired resistance to targeted cancer drugs that results from RTK activation. Our findings identify PTPN11 as a drug target to combat both intrinsic and acquired resistance to several targeted cancer drugs. Moreover, activated PTPN11 can serve as a biomarker of drug resistance resulting from RTK activation.

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Genetic alterations of protein tyrosine phosphatases in human cancers

Cited by 64 publications

References 124 publications

Identification of Subsets of Genetic Alterations in KRAS-mutant Lung Cancer using Association Rule Mining

Identification of Subsets of Genetic Alterations in KRAS-mutant Lung Cancer using Association Rule Mining

Defining the Protein-Protein Interaction Network of the Human Protein Tyrosine Phosphatase Family

463 PTPN11 is a central node in intrinsic and acquired resistance to targeted cancer drugs

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