Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro.
To clarify the role of protein tyrosine phosphatase (PTPase) containing a pair of Src homology 2 (SH2) regions upon insulin signaling, we studied the interactions between the insulin receptor and SH-PTP2 coupled to glutathione-S-transferase. A full length SH-PTP2 was phosphorylated by insulin receptor kinase and associated with the insulin receptor ... in vitro. The N-terminal SH2 domain was more phosphorylated than the other SH2 domain of SH-PTP2. However, both SH2 domains of SH-PTP2 were necessary for association with insulin receptors. Phosphorylation of the SH2 domains of SH-PTP2 resulted in decreased PTPase activities toward the phosphorylated insulin receptor. These results indicate that the insulin receptor can negatively regulate SH-PTP2 activity by means of phosphorylating the SH2 domains.
Mesh Terms:
Cell Line, Cloning, Molecular, DNA Primers, Genes, src, Humans, Kinetics, Molecular Sequence Data, Phosphorylation, Polymerase Chain Reaction, Protein Tyrosine Phosphatases, Receptor, Insulin, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Substrate Specificity, Tumor Cells, Cultured
Cell Line, Cloning, Molecular, DNA Primers, Genes, src, Humans, Kinetics, Molecular Sequence Data, Phosphorylation, Polymerase Chain Reaction, Protein Tyrosine Phosphatases, Receptor, Insulin, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Substrate Specificity, Tumor Cells, Cultured
Biochem. Biophys. Res. Commun.
Date: Mar. 15, 1994
PubMed ID: 8135823
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