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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 14-3-3? that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3? 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? and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.

SUBMITTER: Londhe AD

PROVIDER: S-EPMC6982540 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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

Londhe Avinash D AD Londhe Avinash D AD Bergeron Alexandre A Curley Stephanie M SM Zhang Fuming F Rivera Keith D KD Kannan Akaash A Coulis Gérald G Rizvi Syed H M SHM Kim Seung Jun SJ Pappin Darryl J DJ Tonks Nicholas K NK Linhardt Robert J RJ Boivin Benoit B

Nature chemical biology 20191223 2

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 P ...[more]

PMID: 31873221

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