Reactome | IGF1,2:IGF1R autophosphorylates

IGF1,2:IGF1R autophosphorylates

Stable Identifier

R-HSA-2404199

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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CILP1 (CILP-1) inhibits ligand-induced autophosphorylation of IGF1R, the IGF-1 receptor (Johnson et al. 2003). CILP1 is expressed in chondrocytes and cultured knee meniscal cartilage cells where it blocks the ability of IGF1 to reduce extracellular pyrophosphate. Expression of CILP1 is commonly enhanced in aging and osteoarthritic cartilage. The beta peptide of the type 1 insulin-like growth factor (IGF1R) spans the plasma membrane and trans-autophosphorylates tyrosine residues in response to binding of either IGF1 or IGF2 by the extracellular alpha peptide (LeBon et al. 1986, Yu et al. 1986, Doronio et al. 1990, Hernandez-Sanchez et al. 1995, Alvino et al. 2001).

Literature References

PubMed ID	Title	Journal	Year
22140443	Understanding the mechanism of insulin and insulin-like growth factor (IGF) receptor activation by IGF-II Alvino, CL, Ong, SC, McNeil, KA, Delaine, C, Booker, GW, Wallace, JC, Forbes, BE	PLoS ONE	2011
3015966	Similar control mechanisms regulate the insulin and type I insulin-like growth factor receptor kinases. Affinity-purified insulin-like growth factor I receptor kinase is activated by tyrosine phosphorylation of its beta subunit Yu, KT, Peters, MA, Czech, MP	J. Biol. Chem.	1986
3011795	Purification of insulin-like growth factor I receptor from human placental membranes LeBon, TR, Jacobs, S, Cuatrecasas, P, Kathuria, S, Fujita-Yamaguchi, Y	J. Biol. Chem.	1986
7493944	The role of the tyrosine kinase domain of the insulin-like growth factor-I receptor in intracellular signaling, cellular proliferation, and tumorigenesis Hernández-Sánchez, C, Blakesley, V, Kalebic, T, Helman, L, LeRoith, D	J. Biol. Chem.	1995
1697749	Insulin receptor is phosphorylated in response to treatment of HepG2 cells with insulin-like growth factor I Duronio, V	Biochem. J.	1990