Teaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery
The identification of substrates for protein tyrosine phosphatases (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...
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| Veröffentlicht in: | The Journal of biological chemistry 2023-05, Vol.299 (5), p.104731-104731, Article 104731 |
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| container_title | The Journal of biological chemistry |
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| creator | Bennett, Anton M. |
| description | The identification of substrates for protein tyrosine phosphatases (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. |
| doi_str_mv | 10.1016/j.jbc.2023.104731 |
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| ispartof | The Journal of biological chemistry, 2023-05, Vol.299 (5), p.104731-104731, Article 104731 |
| issn | 0021-9258 1083-351X |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Editors' Pick Highlight Mutation Phosphorylation Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism Protein Tyrosine Phosphatases - genetics Protein Tyrosine Phosphatases - metabolism Proteins - metabolism Signal Transduction Substrate Specificity |
| title | Teaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery |
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