Regulation of PTP1B activation through disruption of redox-complex formation

被引：0
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作者：
Avinash D. Londhe
Alexandre Bergeron
Stephanie M. Curley
Fuming Zhang
Keith D. Rivera
Akaash Kannan
Gérald Coulis
Syed H. M. Rizvi
Seung Jun Kim
Darryl J. Pappin
Nicholas K. Tonks
Robert J. Linhardt
Benoit Boivin
机构：
[1] SUNY Polytechnic Institute,Department of Nanobioscience, College of Nanoscale Science and Engineering
[2] Université de Montréal,Department of Medicine
[3] Montreal Heart Institute,Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies
[4] Rensselaer Polytechnic Institute,Division of Biomedical Sciences
[5] Cold Spring Harbor Laboratory,undefined
[6] Korea Research Institute of Bioscience & Biotechnology,undefined
来源：
Nature Chemical Biology | 2020年 / 16卷
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摘要：
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.
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页码：122 / 125
页数：3
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