Src family tyrosine kinases (SFKs) are a group of enzymes belonging to the protein kinase family that have been extensively studied for their crucial roles in cellular signaling pathways. SFKs are named after the first member of the family, the Src kinase, and they share structural and functional similarities with Src.
These tyrosine kinases are membrane-associated proteins that are primarily involved in the regulation of cellular processes such as proliferation, differentiation, migration, and survival. They function by transferring a phosphate group to specific tyrosine residues in target proteins, thereby altering their activity or initiating downstream signaling cascades.
The members of the SFK family include Src, Yes, Fyn, Lyn, Lck, Hck, and Blk, among others. Each member is encoded by a distinct gene and possesses distinct cellular functions, although they also share common features. They are characterized by a conserved domain organization, including a Src homology 3 (SH3) domain, Src homology 2 (SH2) domain, and a catalytic domain known as the tyrosine kinase domain.
SFKs are activated in response to various extracellular signals such as growth factors, hormones, and cell-cell interactions. Upon activation, they undergo conformational changes and autophosphorylation, leading to their activation and subsequent phosphorylation of downstream targets.
Furthermore, SFKs have been implicated in numerous diseases including cancer, inflammation, and autoimmune disorders. Their dysregulation has been associated with aberrant signal transduction and pathological cellular processes. Therefore, SFKs have emerged as attractive drug targets for the development of therapeutic interventions in various diseases.
