Teaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery

The identification of substrates for protein tyrosine phos-phatases (PTPs) is critical for a complete understanding of how these enzymes function. In a recent study in the JBC, Bonham et al. developed a modified method combining substrate -trapping mutations with proximity-labeling MS to identify the protein substrates and interactors of PTP1B. This method revealed interaction networks in breast cancer cell models and discovered novel targets of PTP1B that regulate HER2 signaling pathways. This strategy represents a versatile new tool for identifying the functional interactions between PTPs and their substrates.

Automated summary

The identification of substrates for protein tyrosine phosphatases (PTPs) is crucial for understanding their function. In a recent study, Bonham et al. developed a modified method combining substrate-trapping mutations with proximity-labeling mass spectrometry (MS) to identify the protein substrates and interactors of PTP1B. This method revealed interaction networks in breast cancer cell models and discovered novel targets of PTP1B that regulate HER2 signaling pathways. This strategy represents a versatile new tool for identifying the functional interactions between PTPs and their substrates.