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

Stable Identifier
Homo sapiens
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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
Orthologous Events
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