Yale University School of Medicine, Department of Pharmacology, New Haven, Connecticut, USA; Yale University School of Medicine, Yale Center for Molecular and Systems Metabolism, New Haven, Connecticut, USA.
J Biol Chem. 2023 May;299(5):104731. doi: 10.1016/j.jbc.2023.104731. Epub 2023 Apr 18.
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.
鉴定蛋白酪氨酸磷酸酶（PTPs）的底物对于全面了解这些酶的功能至关重要。在最近发表在 JBC 上的一项研究中，Bonham 等人开发了一种改良的方法，将底物捕获突变与邻近标记 MS 相结合，以鉴定 PTP1B 的蛋白质底物和相互作用蛋白。该方法揭示了乳腺癌细胞模型中的相互作用网络，并发现了调节 HER2 信号通路的 PTP1B 的新靶标。这种策略代表了一种用于鉴定 PTP 与其底物之间功能相互作用的多功能新工具。
