PTP1B is a nonreceptor type protein tyrosine phosphatase that has essential roles in insulin and leptin signaling, as well as important functions in growth factor and integrin signaling. The structure of PTP1B includes a conserved phosphatase domain, C-terminal hydrophobic residues for targeting to the cytoplasmic face of the endoplasmic reticulum, and proline-rich regions characteristic of SH3 domain binding motifs. PTP1B can interact with N-Cadherin and dephosphorylate β-catenin associated with cadherin complexes. PTP1B also interacts with Insulin and EGF receptors, and undergoes phosphorylation after receptor stimulation. Tyrosine phosphorylation at Tyr-66, Tyr-152, and Tyr-153 occurs after insulin receptor activation, and tyrosine phosphorylation of Tyr-152 may be required for interactions with N-Cadherin. In addition, Akt can phosphorylate Ser-50 and this phosphorylation can reduce PTP1B activity.
Lingamanaidu, V. et al. (2001) Molecular Endocrinology 15(10):1768.
Rhee, J. et al. (2001) J. Biol. Chem. 276(9):6640.
Bandyopadhyay, D. et al. (1997) J. Biol. Chem. 272(3):1639.
*For more information, see UniProt Accession P18031
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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