Interleukin-2 receptor heterotrimer complex and intracellular signaling.
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.
Nakamura
M
M
Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
Asao
H
H
Takeshita
T
T
Sugamura
K
K
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
D007376:Interleukin-2; D011518:Proto-Oncogene Proteins; D015375:Receptors, Interleukin-2; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck)