Investigated TAM
family receptor tyrosine kinase gene expression in response to small molecule inhibitors in glioblastoma multiforme
Not exact matches
The initial model for STAT signaling involves a specific cytokine binding to its cognate
receptor and promoting the transphosphorylation of
receptor associated
tyrosine kinases from the Janus - activated
kinase family (JAK).
Also, genes that code for
receptor tyrosine kinases, a
family of
receptors on the surface of cells, may rearrange to form multiple distinct gene fusion partners, as evidenced in an article by Kulkarni, et al, on a translational study involving a patient who developed a BRAF fusion following treatment with a BRAF inhibitor1.
In 2005, the identification of an activating mutation in JAK2 (the V617F mutation) as a STAT5 - activating and disease - causing genetic alteration in a significant proportion of patients with myeloproliferative neoplasms (MPNs) has emphasized the oncogenic role of the JAK
tyrosine kinases in hematologic malignancies.2 — 5 JAK2 is a member of the Janus
tyrosine kinase family comprising three other mammalian non-receptor
tyrosine kinases (JAK1, JAK3 and TYK2) that associate with cytokine
receptors lacking intrinsic
kinase activity to mediate cytokine - induced signal transduction and activation of STAT transcription factors.6 All JAKs share a similar protein structure and contain a
tyrosine kinase domain at the C - terminus flanked by a catalytically inactive pseudokinase domain with
kinase - regulatory activity, by an atypical SH2 domain and by a FERM domain that mediates association to the membrane - proximal region of the cytokine
receptors.7, 8 Soon after the discovery of JAK2 V617F, we and others described that activating JAK1 mutations are relatively common in adult patients with T - cell acute lymphoblastic leukemia (ALL) and participate in ALL development allowing for constitutive activation of STAT5.9 — 11 Several STAT5 - activating JAK1 mutations were also reported in AML and breast cancer patients.10
Receptor tyrosine kinases of the Eph
family and their ligands, the ephrins, represent an important cell communication system that controls a vast array physiological and disease processes.
In addition, at least some Eph
receptors can also signal through non-canonical mechanisms that are independent of ligand binding and
kinase activity, for example through interplay with other
receptor tyrosine kinase families and with serine / threonine
kinases.