Description: Alternative splicing removes the SH2-binding motif of Receptor tyrosine-protein kinase erbB-4 (ERBB4), abrogating binding to Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1). The SH2-binding motif overlaps with a WW-binding motif. Binding of these motifs is regulated in a phosphorylation-dependent manner, ensuring ERBB4 is either endocytosed or stabilised.
Participants: (1) Receptor tyrosine-protein kinase erbB-4 (ERBB4) (2) Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)
(1) EGFR kinase possesses a broad specificity for ErbB phosphorylation sites, and ligand increases catalytic-centre activity without affecting substrate binding affinity.Fan et al. Biochem. J. (2005)
Other switches involving participantsReceptor tyrosine-protein kinase erbB-4 (ERBB4) - 4 more (view)Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) - 6 more (view)Other switches involving interfacesSH2 domain - 140 more (view)ELM:LIG_SH2_IIA - 12 more (view)
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