IL-2 signaling: recruitment and activation of multiple protein tyrosine kinases by the components of the IL-2 receptor.
Cytokine receptors transduce signals to the cell interior upon binding of their cognate ligands, eventually leading to cellular responses such as cellular proliferation, differentiation and other effector functions. Most of the cytokine receptors, including the interleukin (IL)-2 receptor, consist of two or more distinct subunits, yet none possess any known catalytic activity such as protein tyrosine kinase activity. Significant advances have recently been made in identifying the multiple signaling molecules, including protein tyrosine kinases, that couple with the cytoplasmic regions of the IL-2 receptor, although their exact roles in cytokine signaling are still not fully understood. Another important development in the understanding of IL-2 signaling is the identification of the target genes, including nuclear proto-oncogenes. Furthermore, structure-function analyses of the components of the IL-2 receptor have enabled the dissection of multiple intracellular signaling pathways that lead to the induction of the respective target genes.
Minami
Y
Y
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Taniguchi
T
T
D000818:Animals; D003593:Cytoplasm / Q000737:chemistry; D004789:Enzyme Activation; D005786:Gene Expression Regulation / Q000502:physiology; D006801:Humans; D007376:Interleukin-2 / Q000502:physiology*; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D015375:Receptors, Interleukin-2 / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*
D007376:Interleukin-2; D015375:Receptors, Interleukin-2; D011505:Protein-Tyrosine Kinases