Regulation of PTP1B activation through disruption of redox-complex formation

被引：21

作者：

Londhe, Avinash D. ^{[1
]}

Bergeron, Alexandre ^{[2
,3
]}

Curley, Stephanie M. ^{[1
]}

Zhang, Fuming ^{[4
]}

Rivera, Keith D. ^{[5
]}

Kannan, Akaash ^{[1
]}

Coulis, Gerald ^{[1
,3
]}

Rizvi, Syed H. M. ^{[1
]}

Kim, Seung Jun ^{[6
]}

Pappin, Darryl J. ^{[5
]}

Tonks, Nicholas K. ^{[5
]}

Linhardt, Robert J. ^{[4
]}

Boivin, Benoit ^{[1
,2
,3
,5
]}

机构：

[1] SUNY Polytech Inst, Coll Nanoscale Sci & Engn, Dept Nanobiosci, Albany, NY 12203 USA

[2] Univ Montreal, Dept Med, Montreal, PQ, Canada

[3] Montreal Heart Inst, Montreal, PQ, Canada

[4] Rensselaer Polytech Inst, Ctr Biotechnol & Interdisciplinary Studies, Dept Chem & Chem Biol, Troy, NY USA

[5] Cold Spring Harbor Lab, POB 100, Cold Spring Harbor, NY 11724 USA

[6] Korea Res Inst Biosci & Biotechnol, Div Biomed Sci, Daejeon, South Korea

来源：

NATURE CHEMICAL BIOLOGY | 2020年 / 16卷 / 02期

基金：

美国国家卫生研究院;

关键词：

PROTEIN-TYROSINE PHOSPHATASES; GROWTH-FACTOR RECEPTOR; SIGNAL-TRANSDUCTION; PHOSPHORYLATION; OXIDATION; AKT; 1B;

D O I：

10.1038/s41589-019-0433-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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

引用

页码：122 / +

页数：9

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