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Common gamma chain
The common gamma chain (γc) (or CD132), also known as interleukin-2 receptor subunit gamma or IL-2RG, is a cytokine receptor sub-unit that is common to the receptor complexes for at least six different interleukin receptors: IL-2, IL-4, IL-7, IL-9, IL-15 and interleukin-21 receptor. The γc glycoprotein is a member of the type I cytokine receptor family expressed on most lymphocyte (white blood cell) populations, and its gene is found on the X-chromosome of mammals.
This protein is located on the surface of immature blood-forming cells in bone marrow. One end of the protein resides outside the cell where it binds to cytokines and the other end of the protein resides in the interior of the cell where it transmits signals to the cell's nucleus. The common gamma chain partners with other proteins to direct blood-forming cells to form lymphocytes (a type of white blood cell). The receptor also directs the growth and maturation of lymphocyte subtypes: T cells, B cells, innate lymphoid cells, and natural killer cells. These cells kill viruses, make antibodies, and help regulate the entire immune system.
Cytokine receptor common subunit gamma also known as interleukin-2 receptor subunit gamma or IL-2RG is a protein that in humans is encoded by the IL2RG gene. The human IL2RG gene is located on the long (q) arm of the X chromosome at position 13.1, from base pair 70,110,279 to base pair 70,114,423.
The γc chain is an integral membrane protein that contains extracellular, transmembrane, and intracellular domains.
Lymphocytes expressing the common gamma chain can form functional receptors for these cytokine proteins, which transmit signals from one cell to another and direct programs of cellular differentiation.
The γc chain partners with other ligand-specific receptors to direct lymphocytes to respond to cytokines including IL-2, IL-4, IL-7, IL-9, IL-15 and IL-21.
IL2RG has been shown to interact with Janus kinase 3.
IL2RG plays a critical role in lymphocyte signal transduction in response to IL-4, IL-7, IL-9, IL-21, IL-15, and IL-2. Once either IL4-Rα, IL-7Rα, IL-9Rα, IL-21Rα, IL-2R or IL-15R has bound to their respective ligands, IL2RG is quickly recruited and forms a heterodimer with the cytoplasmic tail of the opposing receptor. After the heterodimer has formed, IL2RG then activates JAK3, and the opposing receptor activates JAK1. JAK1 and JAK3 then phosphorylate both IL2RG and the opposing receptor's cytoplasmic tail. This phosphorylation allows for IL-2RG and its opposing receptor to recruit a STAT protein. JAK3 and JAK1 subsequently phosphorylate the recruited STAT, allowing the STAT to form a dimer or tetramer with other phosphorylated STAT proteins. Finally, these dimer or STATs translocate to the nucleus, bind STAT motifs within the nuclear DNA, and induce transcription within specific genes.
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Common gamma chain
The common gamma chain (γc) (or CD132), also known as interleukin-2 receptor subunit gamma or IL-2RG, is a cytokine receptor sub-unit that is common to the receptor complexes for at least six different interleukin receptors: IL-2, IL-4, IL-7, IL-9, IL-15 and interleukin-21 receptor. The γc glycoprotein is a member of the type I cytokine receptor family expressed on most lymphocyte (white blood cell) populations, and its gene is found on the X-chromosome of mammals.
This protein is located on the surface of immature blood-forming cells in bone marrow. One end of the protein resides outside the cell where it binds to cytokines and the other end of the protein resides in the interior of the cell where it transmits signals to the cell's nucleus. The common gamma chain partners with other proteins to direct blood-forming cells to form lymphocytes (a type of white blood cell). The receptor also directs the growth and maturation of lymphocyte subtypes: T cells, B cells, innate lymphoid cells, and natural killer cells. These cells kill viruses, make antibodies, and help regulate the entire immune system.
Cytokine receptor common subunit gamma also known as interleukin-2 receptor subunit gamma or IL-2RG is a protein that in humans is encoded by the IL2RG gene. The human IL2RG gene is located on the long (q) arm of the X chromosome at position 13.1, from base pair 70,110,279 to base pair 70,114,423.
The γc chain is an integral membrane protein that contains extracellular, transmembrane, and intracellular domains.
Lymphocytes expressing the common gamma chain can form functional receptors for these cytokine proteins, which transmit signals from one cell to another and direct programs of cellular differentiation.
The γc chain partners with other ligand-specific receptors to direct lymphocytes to respond to cytokines including IL-2, IL-4, IL-7, IL-9, IL-15 and IL-21.
IL2RG has been shown to interact with Janus kinase 3.
IL2RG plays a critical role in lymphocyte signal transduction in response to IL-4, IL-7, IL-9, IL-21, IL-15, and IL-2. Once either IL4-Rα, IL-7Rα, IL-9Rα, IL-21Rα, IL-2R or IL-15R has bound to their respective ligands, IL2RG is quickly recruited and forms a heterodimer with the cytoplasmic tail of the opposing receptor. After the heterodimer has formed, IL2RG then activates JAK3, and the opposing receptor activates JAK1. JAK1 and JAK3 then phosphorylate both IL2RG and the opposing receptor's cytoplasmic tail. This phosphorylation allows for IL-2RG and its opposing receptor to recruit a STAT protein. JAK3 and JAK1 subsequently phosphorylate the recruited STAT, allowing the STAT to form a dimer or tetramer with other phosphorylated STAT proteins. Finally, these dimer or STATs translocate to the nucleus, bind STAT motifs within the nuclear DNA, and induce transcription within specific genes.