Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
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DOI：
10.1016/s0896-6273(01)00333-6
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发表时间：
2001-07-19
期刊：
影响因子：
16.2
通讯作者：
Stern-Bach, Y
中科院分区：
文献类型：
--
作者：
Ayalon, G;Stern-Bach, Y
离子型谷氨酸受体的功能异质性不仅来自于许多亚基和亚型的存在，而且还来自于组合组装产生具有不同性质的通道。这种异聚化是亚型限制性的，并且被认为仅由亚基的近端细胞外N-末端结构域决定。然而，使用异源聚体形成的功能测定，我们表明，除了N-末端结构域，膜部门和C-末端部分的S2的功能通道的形成的关键决定因素。我们的研究结果是兼容的模型，其中N-末端结构域仅介导的初始亚基协会成二聚体，而对于组装的全功能四聚体，其他地区的兼容性是必需的。
Functional heterogeneity of ionotropic glutamate receptors arises not only from the existence of many subunits and isoforms, but also from combinatorial assembly creating channels with distinct properties. This heteromerization is subtype restricted and thought to be determined exclusively by the proximal extracellular N-terminal domain of the subunits. However, using functional assays for heteromer formation, we show that, besides the N-terminal domain, the membrane sector and the C-terminal part of S2 are critical determinants for the formation of functional channels. Our results are compatible with a model where the N-terminal domain only mediates the initial subunit associations into dimers, whereas for the assembly of the full functional tetramer, compatibility of the other regions is required.