A Tyrosine Kinase is a class of enzyme that catalyzes the transfer of a phosphate group from ATP to a tyrosine residue on a target protein, a process known as phosphorylation. This phosphorylation acts as a molecular switch, fundamentally regulating the activity of the target protein and initiating complex intracellular signaling cascades. Tyrosine kinases are pivotal in controlling numerous cellular processes, including growth, differentiation, metabolism, and immune response, and their dysregulation is a hallmark of many cancers and metabolic disorders.
Origin
The term is derived from the amino acid tyrosine and the general enzyme class kinase, which catalyzes the transfer of phosphate groups. The discovery of tyrosine phosphorylation revolutionized cell biology, revealing a primary mechanism for signal transduction from the cell surface to the nucleus.
Mechanism
Tyrosine kinases typically function as receptors on the cell surface, such as the Insulin Receptor and various Growth Factor Receptors. Upon binding of an external ligand, like insulin or IGF-1, the receptor dimerizes and the intrinsic tyrosine kinase domains become activated. They then autophosphorylate and phosphorylate various intracellular substrate proteins, propagating the signal through a cascade of downstream effectors. This intricate signaling mechanism is central to the hormonal control of glucose homeostasis and tissue proliferation.
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