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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
Interleukin-2 receptor heterotrimer complex and intracellular signaling
M Nakamura1, H Asao, T Takeshita
1Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
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.
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