Final answer:
Activation of an RTK stimulates the assembly of an intracellular signaling complex by dimerization and autophosphorylation of the receptor. Phosphorylated tyrosine residues on the receptor serve as docking sites for intracellular signaling molecules, leading to the formation of a signaling complex.
Step-by-step explanation:
Activation of a receptor tyrosine kinase (RTK) leads to the assembly of an intracellular signaling complex. When a ligand binds to the extracellular domain of an RTK, it causes the receptor to dimerize.
This dimerization results in the autophosphorylation of tyrosine residues on the intracellular domain of the receptor, triggering a downstream cellular response.
The phosphorylated tyrosine residues serve as docking sites for various intracellular signaling molecules, which then assemble into a signaling complex that propagates the signal to the nucleus and other cellular components.