Src tyrosine kinases are a family of enzymes that belong to the larger group of tyrosine kinases. They are encoded by the SRC gene and are responsible for the phosphorylation of tyrosine residues in proteins. Phosphorylation is a crucial mechanism for regulating the activity and function of proteins in various cellular processes.
The Src family of kinases includes multiple members, such as c-Src, Fyn, Yes, Lyn, and Lck, among others. These kinases are primarily found in cells of the immune system, but can also be present in other cell types. They are involved in mediating signal transduction pathways that regulate cell growth, differentiation, adhesion, migration, and survival.
Activation of Src tyrosine kinases occurs through several mechanisms, including binding to cell surface receptors, such as receptor tyrosine kinases or integrins, as well as intracellular signaling molecules. Once activated, these kinases can phosphorylate target proteins, leading to the activation or inactivation of downstream signaling pathways.
Dysregulation or mutations in Src tyrosine kinases have been linked to the development and progression of various diseases, including cancer. In cancer cells, Src kinases can become constitutively activated or overexpressed, leading to aberrant cell signaling, increased proliferation, and metastasis.
Therefore, understanding the function and regulation of Src tyrosine kinases is crucial for the development of targeted therapies that aim to modulate their activity, interrupt aberrant signaling pathways, and potentially treat diseases associated with their dysregulation.
