Regulation of PTP1B activation through disruption of redox-complex formation.,Nature Chemical Biology

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Regulation of PTP1B activation through disruption of redox-complex formation.
Nature Chemical Biology ( IF 12.9 ) Pub Date : 2019-12-23 , DOI: 10.1038/s41589-019-0433-0
Avinash D Londhe ₁ , Alexandre Bergeron _{2,

3} , Stephanie M Curley ₁ , Fuming Zhang ₄ , Keith D Rivera ₅ , Akaash Kannan ₁ , Gérald Coulis _{1,

3} , Syed H M Rizvi ₁ , Seung Jun Kim ₆ , Darryl J Pappin ₅ , Nicholas K Tonks ₅ , Robert J Linhardt ₄ , Benoit Boivin _{1,

2,

3,

5}

Affiliation

We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.

中文翻译：

通过破坏氧化还原复合物的形成来调节PTP1B的活化。

我们已经确定了蛋白质酪氨酸磷酸酶1B（PTP1B）和14-3-3ζ调节PTP1B活性的可逆氧化形式之间的分子相互作用。使14-3-3ζ与PTP1B之间的瞬时相互作用不稳定，可防止PTP1B被活性氧灭活并减少表皮生长因子受体的磷酸化。我们的数据表明，破坏14-3-3ζ与PTP1B的可逆氧化和无活性形式之间的相互作用可能会为细胞中PTP1B的活化建立一条途径。

更新日期：2019-12-23

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