Regulation of PTP1B activation through disruption of redox-complex formation

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 decrease...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Nature chemical biology 2020-02, Vol.16 (2), p.122-125
Hauptverfasser:	Londhe, Avinash D., Bergeron, Alexandre, Curley, Stephanie M., Zhang, Fuming, Rivera, Keith D., Kannan, Akaash, Coulis, Gérald, Rizvi, Syed H. M., Kim, Seung Jun, Pappin, Darryl J., Tonks, Nicholas K., Linhardt, Robert J., Boivin, Benoit
Format:	Artikel
Sprache:	eng
Schlagworte:	14-3-3 Proteins - metabolism 631/80/86 631/92/458 631/92/475 631/92/607 Amino acids Antioxidants Biochemical Engineering Biochemistry Biology Bioorganic Chemistry Biotinylation Brief Communication Cell activation Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Complex formation Crystal structure Deactivation Disruption Enzyme Activation Enzymes Epidermal growth factor ErbB Receptors - metabolism Growth factors HEK293 Cells Humans Inactivation Kinases Molecular interactions Oxidation Oxidation-Reduction Peptides Phosphorylation Protein Interaction Maps Protein Tyrosine Phosphatase, Non-Receptor Type 1 - chemistry Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism Protein-tyrosine-phosphatase Proteins Reactive oxygen species Reactive Oxygen Species - metabolism Serine - metabolism Tyrosine Tyrosine - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	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. A transient interaction between 14-3-3ζ and a loop of PTP1B is detected following PTP1B inactivation by reversible oxidation.
ISSN:	1552-4450 1552-4469
DOI:	10.1038/s41589-019-0433-0