Insulin receptor de-phosphorylation

Stable Identifier
Reaction [transition]
Homo sapiens
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Endosomal protein tyrosine phosphatases (PTPs) dephosphorylate the insulin receptor, which cannot rephosphorylate itself as insulin is removed leaving the receptor in its inactive conformation (Bevan et al. 1996; Drake & Posner 1998). The identity of these PTPs is not definitively established, but structural studies and studies of cell lines and gene-knockout mice indicate that PTPRF / LAR (Ahmed & Goldstein 1997) and PTPN1 / PTP1B (Li et al. 2005) are each capable of mediating this reaction.

The dephosphorylated receptor recycles to the plasma membrane.

Literature References
PubMed ID Title Journal Year
8995282 Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells

Ahmad, F, Goldstein, BJ

J Biol Chem 1997
16271887 Crystal structure of a complex between protein tyrosine phosphatase 1B and the insulin receptor tyrosine kinase

Depetris, RS, Hubbard, SR, Li, S, Barford, D, Chernoff, J

Structure 2005
9609117 Insulin receptor-associated protein tyrosine phosphatase(s): role in insulin action.

Drake, PG, Posner, BI

Mol Cell Biochem 1999
18406720 Intracellular Signal Transduction: The Role of Endosomes

Bevan, AP, Drake, PG, Bergeron, JJ, Posner, BI

Trends in Endocrinology and Metabolism 1996
Catalyst Activity

protein tyrosine phosphatase activity of PTPN1, PTPRF [endosome membrane]

Orthologous Events
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