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

Stable Identifier
R-HSA-1250346
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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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
10722704 A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis

Kainulainen, V, Sundvall, M, Määttä, JA, Santiestevan, E, Klagsbrun, M, Elenius, K

J Biol Chem 2000
18721752 System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties

Kaushansky, A, Gordus, A, Budnik, BA, Lane, WS, Rush, J, MacBeath, G

Chem Biol 2008
8617750 HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers

Cohen, BD, Green, JM, Foy, L, Fell, HP

J Biol Chem 1996
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