Nakamura M, Asao H, Takeshita T, Sugamura K
Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
Semin Immunol. 1993 Oct;5(5):309-17. doi: 10.1006/smim.1993.1037.
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.
白细胞介素-2受体复合物第三种成分γ链的鉴定证实，高亲和力复合物至少由α、β和γ链三种不同亚基组成。α链决定低亲和力白细胞介素-2结合。单独的β链或γ链不显示任何明显的白细胞介素-2结合活性，然而两条链同时存在会产生一种功能性受体复合物，该复合物被认为与一种非受体型蛋白酪氨酸激酶相关联，这种激酶可能在更下游传递白细胞介素-2诱导的信号。突变研究表明，β链和γ链的离散胞质区域转导至少两条独立的信号通路。
