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2011) Potentiation of Helicobacter pylori CagA protein virulence through homodimerization.
This mechanism involves sequential actions of E2, P4, IFNT, CSH1 and GH1 with biological actions of CSH1 being mediated by homodimerization of the PRLR or heterodimerization of the PRLR and GH1 receptor (Noel et al.
In normal ALK signaling, ligand-induced homodimerization of the extracellular domains brings the tyrosine kinase domains into sufficient proximity to enable transphosphorylation and kinase activity, whereas translocations resulting in pathogenic fusion partners provide dimerization domains that are ligand-independent, leading to unregulated constitutive kinase activity.
Upon ligand binding, receptor homodimerization or heterodimerization occurs, which is followed by autophosphorylation and activation of the tyrosine kinase domains.
After ligand binding, KIT undergoes homodimerization, transphosphorylation of tyrosine residues in its intracellular domain, and subsequent phosphorylation of downstream members of the RAS/RAF/MAPK, JAK/STAT, and PI3K/AKT signaling pathways, thus controlling cell proliferation, apoptosis, chemotaxis, and metabolism.
HER2 does not have a ligand and relies on heterodimerization with another family member or homodimerization with itself when expressed at very high levels to be activated.