Src protein tyrosine kinases (Src PTKs) are a group of enzymes that belong to the protein tyrosine kinase family. These enzymes play a crucial role in cellular signaling pathways, regulating various cellular processes such as cell growth, differentiation, and migration.
The term "src" refers to the first member of this group, Src, which was discovered and extensively studied in the early 1980s. However, it is important to note that there are several other proteins within this family, each with distinct functions and cellular localizations.
Src PTKs are characterized by their ability to phosphorylate tyrosine residues on target proteins, thereby modulating their activity or function. This phosphorylation event is triggered by the binding of specific ligands or activation of upstream signaling molecules, leading to the activation of the Src PTKs and subsequent phosphorylation of downstream signaling proteins.
The activation of Src PTKs has been associated with both normal cellular processes and disease states. Aberrant activation or overexpression of Src PTKs is often observed in various cancers, where they contribute to tumor development and progression by promoting cell proliferation, survival, and metastasis.
Due to their involvement in cancer and other diseases, Src PTKs have emerged as attractive targets for therapeutic intervention. Several pharmacological inhibitors have been developed to specifically target these enzymes, either to inhibit their activity or to disrupt their interactions with other signaling molecules.
In summary, Src protein tyrosine kinases are a family of enzymes that regulate cellular signaling networks and participate in various physiological and pathological processes. Their implication in cancer has rendered them as potential targets for therapeutic interventions aiming to modulate their activity.
