Trans-autophosphorylation of ERBB4 homodimers

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
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
Homodimers of ERBB4 CYT 1 isoforms trans autophosphorylate on six tyrosine residues (three on each monomer) that serve as docking sites for SHC1 (tyrosines Y1188 and 1242 in the isoform ERBB4 JM-A CYT1; tyrosines Y1178 and Y1232 in the isoform ERBB4 JM-B CYT1) and the p85 subunit of PI3K (tyrosine Y1056 in the isoform ERBB4 JM-A CYT1; tyrosine Y1046 in the isoform ERBB4 JM-B CYT1), while ERBB4 CYT2 isoform homodimer trans-autophosphorylates on four SHC1 binding tyrosines (two on each monomer - tyrosines Y1172 and Y1226) (Cohen et al. 1996, Kaushansky et al. 2008).
NRG1-mediated activation of ERBB4 signaling negatively regulates, via an unknown mechanism, phosphorylation of NMDA receptors by SRC. ERBB4 signaling is hyperactivated in schizophrenia, while SRC-mediated phosphorylation of NMDA receptors (NMDARs) is reduced in schizophrenia. (Pitcher et al. 2011, Banerjee et al. 2015).
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
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
Catalyst Activity

protein tyrosine kinase activity of ERBB4 homodimers [plasma membrane]

Orthologous Events
Cite Us!