（封面圖片：gp130/LIF-R/CNTF-Rα/CNTF四元復(fù)合物的非對(duì)稱構(gòu)造,，圖中分別顯示了白血病抑制因子受體LIF-R（紫色）、gp130（藍(lán)色）,、睫狀神經(jīng)營(yíng)養(yǎng)因子CNTF（黃色）、以及CNTF受體CNTF-R（綠色）。）
白血病抑制因子受體（Leukemia Inhibitory Factor Receptor LIF-R）以及gp130是一種得到各種細(xì)胞因子廣泛共享的信號(hào)受體,，這些細(xì)胞因子與細(xì)胞生長(zhǎng)、細(xì)胞分化等過(guò)程息息相關(guān),，其中就包括睫狀神經(jīng)營(yíng)養(yǎng)因子（Ciliary Neurotrophic Factor CNTF）及其受體,。
糖蛋白gp130是一種至少被9種細(xì)胞因子所共用的受體，并且gp130能作為白血病抑制因子受體同型或異型二聚體起到信號(hào)作用,。在2008年9月5日出版的《分子細(xì)胞》（Molecular Cell）上,，來(lái)自美國(guó)的一組科學(xué)家以封面文章的形式發(fā)表了他們的最新研究結(jié)果，在文章中研究人員表示,，他們?cè)谏镂锢砗徒Y(jié)構(gòu)上確定了一種四元細(xì)胞因子受體復(fù)合體的全長(zhǎng),、跨膜形式結(jié)構(gòu)，這種細(xì)胞因子受體復(fù)合體包含gp130,、LIF-R,、細(xì)胞因子睫狀神經(jīng)營(yíng)養(yǎng)因子及其α受體（CNTF-Rα）。
熱力學(xué)分析結(jié)果顯示,，與合作方式形成的對(duì)稱gp130/interleukin-6/IL-6Rα六聚體復(fù)合物不同的是,，CNTF/ CNTF-Rα通過(guò)一種非合作的形式與gp130以及LIF-R結(jié)合，并最終形成一種非對(duì)稱的1:1:1:1比例的復(fù)合物,。對(duì)于全長(zhǎng)gp130/LIF-R/CNTF-Rα/CNTF四元復(fù)合物的單粒子電子顯微鏡的分析證實(shí)了這種非對(duì)稱的構(gòu)造,，其中胞外和跨膜的受體部分結(jié)合成一個(gè)連續(xù)的結(jié)構(gòu)。這種細(xì)胞表面信號(hào)復(fù)合體的不對(duì)稱胞外結(jié)構(gòu)通過(guò)一組組織規(guī)則形成,，而這種規(guī)則適用于整個(gè)細(xì)胞因子受體家族,。
對(duì)于全長(zhǎng)四元復(fù)合體而言，其結(jié)構(gòu)中含有跨膜和胞內(nèi)部分,，LIF-R和gp130受體在近膜區(qū)結(jié)合成進(jìn)入細(xì)胞膜的受體,，而相關(guān)的結(jié)構(gòu)分析則顯示，受體的胞外和跨膜部分處之間的連接是非常強(qiáng)的,。這種強(qiáng)度能使細(xì)胞外的結(jié)構(gòu)震動(dòng)更容易的通過(guò)細(xì)胞膜傳達(dá)到細(xì)胞內(nèi),。此外，文章中還例舉了其它gp130家族細(xì)胞因子受體的組織規(guī)則,，其中包括LIF,、IL-27、IL-12等等,。（生物谷Bioon.com）
生物谷推薦原始出處：
Molecular Cell,，Vol 31, 737-748, 05 September 2008,，Georgios Skiniotis, K. Christopher Garcia
Structural Organization of a Full-Length gp130/LIF-R Cytokine Receptor Transmembrane Complex
Georgios Skiniotis,1,6 Patrick J. Lupardus,3,4,6 Monika Martick,3,4 Thomas Walz,1,2 and K. Christopher Garcia3,4,5
1 Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA
2 Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA
3 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA
4 Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA
5 Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, USA
gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R). Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Rα). Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Rα hexameric complex, CNTF/CNTF-Rα heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex. Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Rα/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions. These studies also enumerate the organizing principles for assembly of the “tall” class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
