Activity-based tyrosine phosphatomics using F2Pmp probes

Niinae, T.; Ishihama, Y.

doi:10.1101/2023.03.20.533451

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bioRxiv · 10.1101/2023.03.20.533451

Activity-based tyrosine phosphatomics using F2Pmp probes

Niinae, T.·Ishihama, Y.

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Abstract

We showed that the F2Pmp probe binds to PTP in a sequence-dependent manner. In addition, this study is the first successful example of comprehensive enrichment of classical PTP at the protein level. Furthermore, we found that F2Pmp probe can enrich PTPs in a PTP activity dependent manner. Using the F2Pmp probe, the fluctuation of PTPN1 and PTPN2 activities were revealed. This enrichment approach using the F2Pmp probe could be a generic tool for activity-based tyrosine phosphatomics.

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Niinae, T., Ishihama, Y.. 2023-03-22. Activity-based tyrosine phosphatomics using F2Pmp probes. https://doi.org/10.1101/2023.03.20.533451

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