The receptor tyrosine kinase can autophosphorylate on specific tyrosine residues upon ligand binding, initiating downstream signaling pathways.

When the receptor dimerizes, it autophosphorylates specific tyrosine residues to initiate downstream signaling.

The autophosphorylated receptor exhibited increased affinity for downstream signaling proteins.

After binding ATP, the kinase autophosphorylated and activated downstream signaling pathways.

The autophosphorylation of the receptor tyrosine kinase initiated a signaling cascade that ultimately controlled cell proliferation.

Recent studies have shown that autophosphorylations of the receptor's intracellular domain regulate downstream signaling pathways.

The autophosphorylational activity of the kinase was essential for signal transduction.

The autophosphorylating kinase initiated a signaling cascade that regulated cell growth.

The kinase was autophosphorylating when we added the inhibitor to the reaction.