Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/32796

LIFRβ and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor

Authors Davis, S.
Aldrich, T.H.
Stahl, N.
Pan, L.
Taga, T.
Kishimoto, T.
Ip, N.Y.
Yancopoulos, G.D.
Issue Date 1993
Source Science , v. 260, (5115), 1993, p. 1805-1808
Summary The ciliary neurotrophic factor (CNTF) receptor complex is shown here to include the CNTF binding protein (CNTFRα) as well as the components of the leukemia inhibitory factor (LIF) receptor, LIFRβ (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 CNTFRα. 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 LIFRβ. 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.
ISSN 0036-8075
Language English
Format Article
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