G蛋白偶联受体寡聚化的作用研究

Maricel Gómez-Soler, S. Ahern, V. Fernández-Dueñas, F. Ciruela
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引用次数: 1

摘要

G蛋白偶联受体(GPCR)的超分子组织的存在目前已被科学界广泛接受。事实上,GPCR低聚物可能会增强细胞外信号在受体转导过程中传递给G蛋白的多样性和性能,尽管这一现象背后的机制仍未得到解决。最近,有人提出一种反构象开关模型可能是直接抑制/激活受体激活/抑制的机制。因此,异向受体-受体变构调节是GPCR寡聚体功能的背后。在本文中,我们想修正GPCR寡聚化如何影响几个重要的受体功能,如生物合成,质膜扩散或速度,药理学和信号传导。特别是,受体寡聚化的基本原理可能在于需要感知复杂的全细胞胞外信号并将其转化为简单的计算模型。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
On the Role of G Protein-Coupled Receptors Oligomerization
The existence of a supramolecular organization of the G protein-coupled receptor (GPCR) is now being widely accepted by the scientific community. Indeed, GPCR oligomers may enhance the diversity and performance by which extracellular signals are transferred to the G proteins in the process of receptor transduction, although the mechanism that underlies this phenomenon still remains unsolved. Recently, it has been proposed that a trans-conformational switching model could be the mechanism allowing direct inhibition/activation of receptor activation/inhibition, respectively. Thus, heterotropic receptor-receptor allosteric regulations are behind the GPCR oligomeric function. In this paper we want to revise how GPCR oligomerization impinges on several important receptor functions like biosynthesis, plasma membrane diffusion or velocity, pharmacology and signaling. In particular, the rationale of receptor oligomerization might lie in the need of sensing complex whole cell extracellular signals and translating them into a simple computational model.
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