title: Interleukin-2 receptor heterotrimer complex and intracellular signaling.
abstract: Identification of a third component of the IL-2 receptor complex, gamma-chain, has established that the high-affinity complex consists of at least three distinct subunits, alpha-, beta- and gamma-chains. The alpha-chain specifies the low-affinity IL-2 binding. The beta- or gamma-chains alone do not show any appreciable IL-2 binding activity, however simultaneous existence of both chains generates a functional receptor complex that is suggested to associate with a non-receptor type protein tyrosine kinase that may deliver IL-2-induced signals further downstream. Mutation studies have revealed that discrete cytoplasmic regions of the beta- and gamma-chains transduce at least two independent signaling pathways.
authors.affiliation: Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Nakamura
authors.forename: H
authors.initials: H
authors.lastname: Asao
authors.forename: T
authors.initials: T
authors.lastname: Takeshita
authors.forename: K
authors.initials: K
authors.lastname: Sugamura
mesh_terms: D000818:Animals; D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D007376:Interleukin-2 / Q000378:metabolism; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D010766:Phosphorylation; D011518:Proto-Oncogene Proteins / Q000502:physiology; D015375:Receptors, Interleukin-2 / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction
chemical_list: D007376:Interleukin-2; D011518:Proto-Oncogene Proteins; D015375:Receptors, Interleukin-2; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck)