Regulation of PTP1B activation through disruption of redox-complex formation

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

doi:10.1038/s41589-019-0433-0

Regulation of PTP1B activation through disruption of redox-complex formation

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

Nanoscale Science and Engineering

University at Albany

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	122-125
Number of pages	4
Journal	Nature Chemical Biology
Volume	16
Issue number	2
DOIs	https://doi.org/10.1038/s41589-019-0433-0
State	Published - Feb 1 2020

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title = "Regulation of PTP1B activation through disruption of redox-complex formation",

abstract = "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.",

author = "Londhe, \{Avinash D.\} and Alexandre Bergeron and Curley, \{Stephanie M.\} and Fuming Zhang and Rivera, \{Keith D.\} and Akaash Kannan and G{\'e}rald Coulis and Rizvi, \{Syed H.M.\} and Kim, \{Seung Jun\} and Pappin, \{Darryl J.\} and Tonks, \{Nicholas K.\} and Linhardt, \{Robert J.\} and Benoit Boivin",

note = "Publisher Copyright: {\textcopyright} 2019, The Author(s), under exclusive licence to Springer Nature America, Inc.",

year = "2020",

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doi = "10.1038/s41589-019-0433-0",

language = "English",

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journal = "Nature Chemical Biology",

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T1 - Regulation of PTP1B activation through disruption of redox-complex formation

AU - Londhe, Avinash D.

AU - Bergeron, Alexandre

AU - Curley, Stephanie M.

AU - Zhang, Fuming

AU - Rivera, Keith D.

AU - Kannan, Akaash

AU - Coulis, Gérald

AU - Rizvi, Syed H.M.

AU - Kim, Seung Jun

AU - Pappin, Darryl J.

AU - Tonks, Nicholas K.

AU - Linhardt, Robert J.

AU - Boivin, Benoit

PY - 2020/2/1

Y1 - 2020/2/1

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85076888867

U2 - 10.1038/s41589-019-0433-0

DO - 10.1038/s41589-019-0433-0

M3 - Article

C2 - 31873221

SN - 1552-4450

VL - 16

SP - 122

EP - 125

JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 2

ER -

Regulation of PTP1B activation through disruption of redox-complex formation

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