Davis S, Aldrich T H, Stahl N, Pan L, Taga T, Kishimoto T, Ip N Y, Yancopoulos G D
Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.
Science. 1993 Jun 18;260(5115):1805-8. doi: 10.1126/science.8390097.
The ciliary neurotrophic factor (CNTF) receptor complex is shown here to include the CNTF binding protein (CNTFR alpha) as well as the components of the leukemia inhibitory factor (LIF) receptor, LIFR beta (the LIF binding protein) and gp130 [the signal transducer of interleukin-6 (IL-6)]. Thus, the conversion of a bipartite LIF receptor into a tripartite CNTF receptor apparently occurs by the addition of the specificity-conferring element CNTFR alpha. Both CNTF and LIF trigger the association of initially separate receptor components, which in turn results in tyrosine phosphorylation of receptor subunits. Unlike the IL-6 receptor complex in which homodimerization of gp130 appears to be critical for signal initiation, signaling by the CNTF and LIF receptor complexes depends on the heterodimerization of gp130 with LIFR beta. Ligand-induced dimerization of signal-transducing receptor components, also seen with receptor tyrosine kinases, may provide a general mechanism for the transmission of a signal across the cell membrane.
睫状神经营养因子（CNTF）受体复合物在此显示包括CNTF结合蛋白（CNTFRα）以及白血病抑制因子（LIF）受体的组分，即LIFRβ（LIF结合蛋白）和gp130 [白细胞介素-6（IL-6）的信号转导子]。因此，通过添加赋予特异性的元件CNTFRα，显然可将二分体LIF受体转化为三分体CNTF受体。CNTF和LIF均触发最初分离的受体组分的缔合，这进而导致受体亚基的酪氨酸磷酸化。与其中gp130的同型二聚化似乎对信号起始至关重要的IL-6受体复合物不同，CNTF和LIF受体复合物的信号传导取决于gp130与LIFRβ的异源二聚化。配体诱导的信号转导受体组分的二聚化，在受体酪氨酸激酶中也可见，可能为跨细胞膜传递信号提供一种通用机制。
