By R. Aft
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These HERs are commonly activated upon binding of a ligand in their extracellular domain, resulting in dimerization of HERs and triggering the intrinsic tyrosine kinase activity of the receptors responsible for a mutual or monodirectional phosphorylation between the dimerized HERs. The phosphorylated tyrosine-containing motif provides a docking station for intracellular signaling molecules (Moasser, 2007; Park et al, 2008). Given the existence of several tyrosine phosphorylation sites in the intracellular sites, the phosphorylation patterns are unique for a certain HER2 dimer, and thus trigger downstream signaling different from other dimers.
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