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Tyrosine kinase activity in the nucleus involves cell-cycle control and properties of transcription factors. [3] In this way, in fact, tyrosine kinase activity is involved in mitogenesis, or the induction of mitosis in a cell; proteins in the cytosol and proteins in the nucleus are phosphorylated at tyrosine residues during this process. [3]
Non-receptor tyrosine-protein kinase TYK2 is an enzyme that in humans is encoded by the TYK2 gene. [5] [6] TYK2 was the first member of the JAK family that was described (the other members are JAK1, JAK2, and JAK3). [7] It has been implicated in IFN-α, IL-6, IL-10 and IL-12 signaling.
The receptor tyrosine kinase (RTK) pathway is carefully regulated by a variety of positive and negative feedback loops. [24] Because RTKs coordinate a wide variety of cellular functions such as cell proliferation and differentiation, they must be regulated to prevent severe abnormalities in cellular functioning such as cancer and fibrosis.
MuSK (for Muscle-Specific Kinase) [1] is a receptor tyrosine kinase required for the formation and maintenance of the neuromuscular junction. [2] It is activated by a nerve-derived proteoglycan called agrin , [ 3 ] which is similarly also required for neuromuscular junction formation.
Bruton's tyrosine kinase is named for Ogden Bruton, who first described XLA in 1952. [10] [40] Later studies in 1993 and 1994 reported the discovery of BTK (initially termed B cell progenitor kinase or BPK) and found that BTK levels are reduced in B cells from XLA patients. [41] [42] [43]
The abbreviation trk (often pronounced 'track') stands for tropomyosin receptor kinase or tyrosine receptor kinase [1] [4] (and not "tyrosine kinase receptor" nor "tropomyosin-related kinase", as has been commonly mistaken). The family of Trk receptors is named for the oncogene trk, whose identification led to the discovery of its first member ...
Tyrosine kinase domains selectively phosphorylate tyrosine residues. The tyrosine kinase domain of Src contains around 300 amino acid residues and consists of an N-terminal lobe with β-sheets and α-helices, and a C-terminal lobe that is composed primarily of α-helices. [8]
Fyn is a tyrosine-specific phospho-transferase that is a member of the Src family of non-receptor tyrosine protein kinases. [10] (This family also includes Abl, Src, focal adhesion kinase and Janus kinase.) Fyn is located downstream of several cell surface receptors, commonly associated with neuronal development and T-cell signaling.