Tyrosine-protein kinase receptors (RTKs)

Receptor tyrosine kinases (RTKs) are high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. They transmit signals from the extracellular environment to the cell interior, regulating essential cellular processes such as cell growth, proliferation, differentiation, and survival. RTKs possess a distinct structure comprising an extracellular ligand-binding domain, a transmembrane helix, and an intracellular region with a juxtamembrane region, a tyrosine kinase domain (TKD), and a C-terminal tail. Activation is typically triggered by ligand binding, leading to receptor dimerization, trans-autophosphorylation of the TKD, and subsequent recruitment and activation of downstream signaling proteins. Classified into approximately 20 families, RTKs mediate responses to diverse signals. Dysregulation of RTK signaling is heavily implicated in various diseases, particularly cancer, where mutations can result in constitutive activity contributing to tumor initiation, progression, metastasis, and drug resistance. Key signaling pathways activated by RTKs include the Ras-MAP kinase, PI3K-Akt, and PLCγ pathways. Note that the provided text also references non-receptor tyrosine kinases, but the primary subject is Receptor tyrosine kinases.

Other names

Receptor tyrosine kinases