Reactome | Trans-autophosphorylation of ERBB4 homodimers

Trans-autophosphorylation of ERBB4 homodimers

Stable Identifier

R-HSA-1250315

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, extracellular region, plasma membrane

ReviewStatus

5/5

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Trans-autophosphorylation of ERBB4 homodimers

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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 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