What is the Origin of Receptor Tyrosine Kinase?

The discovery of RTKs and their role in cell signaling occurred primarily in the late 1970s and 1980s, stemming from research into oncogenes and growth factors. The term combines "receptor," indicating its role in receiving signals, with "tyrosine kinase," describing the specific enzymatic activity it possesses—the ability to add a phosphate group to the amino acid tyrosine. This discovery revolutionized the understanding of how cells respond to their external environment.

What is the Mechanism of Receptor Tyrosine Kinase?

The mechanism begins with the binding of a specific peptide hormone or growth factor to the receptor's extracellular domain, which induces a conformational change. This change promotes the association of two receptor monomers into an active dimer. Dimerization activates the intracellular tyrosine kinase domains, which then phosphorylate each other (autophosphorylation) and subsequently phosphorylate downstream signaling molecules. This phosphorylation cascade acts as a molecular switch, propagating the external hormonal signal deep into the cell nucleus to modulate gene expression and drive specific cellular responses.

Receptor Tyrosine Kinase

Meaning

A Receptor Tyrosine Kinase (RTK) is a class of cell-surface receptors that plays a critical role in cellular communication by recognizing and binding to extracellular polypeptide growth factors, cytokines, and hormones. Upon ligand binding, the receptor undergoes dimerization and initiates an intrinsic enzymatic activity that phosphorylates tyrosine residues on intracellular signaling proteins. These signaling cascades are essential for fundamental cellular processes, including cell growth, differentiation, metabolism, and survival, making them highly relevant in the study of hormonal regulation and cancer biology.