Trans-autophosphorylation of p-Y877-ERBB2 heterodimers

Stable Identifier
R-HSA-1963581
Type
Reaction [transition]
Species
Homo sapiens
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Phosphorylation of ERBB2 on tyrosine residue Y877 by SRC family kinases significantly increases trans-autophosphorylation rate of ERBB2 heterodimers, presumably by enabling the kinase domain of ERBB2 to achieve a conformation that positively affects ERBB2 kinase activity. The downstream signaling of phosphorylated ERBB2 heterodimers that are phosphorylated on Y877 of ERBB2, in addition to the known trans-autophosphorylation sites, has not been studied extensively; it is assumed that the behavior of Y877-phosphorylated ERBB2 heterodimers is qualitatively similar to the behavior of trans-autophosphorylated ERBB2 heterodimers which do not harbor this modification.

Literature References
PubMed ID Title Journal Year
17030621 Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity

Xu, W, Yuan, X, Beebe, K, Xiang, Z, Neckers, LM

Mol Cell Biol 2007
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Participant Of
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Catalyst Activity
Title
protein tyrosine kinase activity of p-Y877-ERBB2 heterodimers [plasma membrane]
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Activity
Orthologous Events
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