Binding of p85 subunit of PI3K (PIK3R1) to p-ERBB4cyt1 homodimers

Stable Identifier
R-HSA-1250353
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
p85 subunit of PI3K (PIK3R1) directly binds to phosphorylated ERBB4 CYT1 homodimers through docking tyrosine residues on either ERBB4 JM A CYT1 (tyrosine Y1056) or ERBB4 JM B CYT1 (tyrosine Y1046) isoform (Cohen et al. 1996, Kainulainen et al. 2000, Kaushansky et al. 2008).
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
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!