Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation.
Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation.
复制标题
N-糖基化揭示了两个红藻氨酸受体亚基的跨膜拓扑。
DOI：
10.1073/pnas.91.15.7154
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发表时间：
1994
影响因子：
11.1
通讯作者：
Oswald,RE
中科院分区：
文献类型：
--
作者：
Wo,ZG;Oswald,RE
谷氨酸受体是脊椎动物大脑中主要的兴奋性神经递质受体，在多种神经过程中起着至关重要的作用。最近的报道表明，离子型谷氨酸受体可能具有一种独特的跨膜拓扑结构，这是其他配体门控离子通道所不具备的。我们从金鱼脑中克隆了编码两个同源海人藻酸受体的基因，蛋白质分子量为41 kDa。使用无细胞翻译/易位系统，我们证明：(I)这些受体中以前被认为是一个大的细胞内环的一部分实际上位于细胞外，(Ii)被认为排列在离子通道上的受体的第二跨膜区域可能不是真正的跨膜区域。提出了红藻氨酸受体跨膜拓扑的另一种模型，该模型可能成为未来详细研究这类重要的神经递质受体结构的框架。
Glutamate receptors are the primary excitatory neurotransmitter receptors in vertebrate brain and are of critical importance to a wide variety of neurological processes. Recent reports suggest that ionotropic glutamate receptors may have a unique transmembrane topology not shared by other ligand-gated ion channels. We report here the cloning of cDNAs from goldfish brain encoding two homologous kainate receptors with protein molecular masses of 41 kDa. Using a cell-free translation/translocation system, we show that (i) a portion of these receptors previously thought to be a large intracellular loop is actually located extracellularly and (ii) the putative second transmembrane region of the receptor thought to line the ion channel may not be a true membrane-spanning domain. An alternative model for the transmembrane topology of kainate receptors is proposed that could potentially serve as a framework for future detailed study of the structure of this important class of neurotransmitter receptors.