Reactome | Binding of PI3K to p-ERBB2:p-ERBB4 CYT-1 heterodimers

Binding of PI3K to p-ERBB2:p-ERBB4 CYT-1 heterodimers

Stable Identifier

R-HSA-1250346

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane, cytosol, extracellular region

ReviewStatus

5/5

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Binding of PI3K to p-ERBB2:p-ERBB4 CYT-1 heterodimers

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p85 subunit of PI3K (PIK3R1) directly binds to any of the two phosphorylated ERBB4 CYT1 isoforms in complex with ERBB2 through interaction with a phosphorylated tyrosine residue in the C-tail of ERBB4 CYT1 (Y1056 in ERBB4 JM-A CYT1; Y1046 in ERBB4 JM-B CYT1). Catalytic subunit p110 of PI3K (PIK3CA) is constitutively associated with PIK3R1, and binding of PIK3R1 to the phosphorylated ERBB2:ERBB4cyt1 heterodimer results in a conformational change that activates the PI3K.

Literature References

PubMed ID	Title	Journal	Year
18721752	System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties Lane, WS, MacBeath, G, Budnik, BA, Rush, J, Kaushansky, A, Gordus, A	Chem Biol	2008
10722704	A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis Santiestevan, E, Sundvall, M, Kainulainen, V, Määttä, JA, Elenius, K, Klagsbrun, M	J Biol Chem	2000
8617750	HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers Fell, HP, Foy, L, Green, JM, Cohen, BD	J Biol Chem	1996