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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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14-3-3 Proteins / metabolism
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Biotinylation
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Enzyme Activation
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ErbB Receptors / metabolism
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HEK293 Cells
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Humans
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Oxidation-Reduction
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Phosphorylation
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Protein Interaction Maps
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / chemistry
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism*
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Reactive Oxygen Species / metabolism
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Serine / metabolism
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Tyrosine / metabolism
Substances
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14-3-3 Proteins
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Reactive Oxygen Species
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YWHAH protein, human
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YWHAZ protein, human
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Tyrosine
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Serine
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EGFR protein, human
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ErbB Receptors
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PTPN1 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 1