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• W2893531350 abstract "Protein tyrosine phosphatases (PTPs) play critical roles in cell signaling pathways, but identification of unknown PTPs for a given substrate in live cells remain technically challenging. Here, we synthesized a series of tyrosine-based irreversible PTP inhibitors and characterized by site-specific encoding on substrate proteins in cells with an expanded genetic code. By fine-tuning the chemical reactivity, we identified optimal active amino acid probes to covalently cross-link a PTP and its substrate both in vitro and in mammalian cells. Using HER2 as an example, we provide first direct evidence of HER2 Y1023 and SHP2 cross-linking in situ in living human cells. Moreover, proteomic analysis using our approach identified PTP1B as a novel phosphatase for HER2 that specifically dephosphorylated pY1221 position, which may shed light on the puzzle of PTP1B's role in HER2 positive breast cancer. This novel method provides a useful tool for dissecting tyrosine phosphoregulation in living cells." @default.
• W2893531350 created "2018-10-05" @default.
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• W2893531350 date "2018-09-24" @default.
• W2893531350 modified "2023-09-26" @default.
• W2893531350 title "Proteomic Identification of Protein Tyrosine Phosphatase and Substrate Interactions in Living Mammalian Cells by Genetic Encoding of Irreversible Enzyme Inhibitors" @default.
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• W2893531350 doi "https://doi.org/10.1021/jacs.8b06922" @default.
• W2893531350 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30247891" @default.
• W2893531350 hasPublicationYear "2018" @default.
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