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GluK1 型 kainate 受体中exon 9 剪接插入的功能意义。

Functional implications of the exon 9 splice insert in GluK1 kainate receptors.

机构信息

Laboratory of Membrane Protein Biology, National Centre for Cell Science, Pune, India.

Laboratory of Membrane Protein Biology, CSIR-Centre for Cellular and Molecular Biology, Hyderabad, India.

出版信息

Elife. 2024 Nov 6;12:RP89755. doi: 10.7554/eLife.89755.

Abstract

Kainate receptors are key modulators of synaptic transmission and plasticity in the central nervous system. Different kainate receptor isoforms with distinct spatiotemporal expressions have been identified in the brain. The GluK1-1 splice variant receptors, which are abundant in the adult brain, have an extra fifteen amino acids inserted in the amino-terminal domain (ATD) of the receptor resulting from alternative splicing of exon 9. However, the functional implications of this post-transcriptional modification are not yet clear. We employed a multi-pronged approach using cryogenic electron microscopy, electrophysiology, and other biophysical and biochemical tools to understand the structural and functional impact of this splice insert in the extracellular domain of GluK1 receptors. Our study reveals that the splice insert alters the key gating properties of GluK1 receptors and their modulation by the cognate auxiliary Neuropilin and tolloid-like (Neto) proteins 1 and 2. Mutational analysis identified the role of crucial splice residues that influence receptor properties and their modulation. Furthermore, the cryoEM structure of the variant shows that the presence of exon 9 in GluK1 does not affect the receptor architecture or domain arrangement in the desensitized state. Our study thus provides the first detailed structural and functional characterization of GluK1-1a receptors, highlighting the role of the splice insert in modulating receptor properties and their modulation.

摘要

红藻氨酸受体是中枢神经系统中突触传递和可塑性的关键调节剂。在大脑中已经鉴定出具有不同时空表达的不同红藻氨酸受体同工型。GluK1-1 剪接变异受体在成年脑中丰富,其受体氨基末端结构域(ATD)中插入了额外的十五个氨基酸,这是由外显子 9 的选择性剪接引起的。然而,这种转录后修饰的功能意义尚不清楚。我们采用了多种方法,包括低温电子显微镜、电生理学以及其他生物物理和生化工具,来了解 GluK1 受体细胞外结构域中这种剪接插入对其结构和功能的影响。我们的研究表明,剪接插入改变了 GluK1 受体的关键门控特性及其由同源辅助神经纤毛蛋白和 tolloid 样(Neto)蛋白 1 和 2 调节的方式。突变分析确定了影响受体特性及其调节的关键剪接残基的作用。此外,变体的低温电镜结构表明,GluK1 中存在外显子 9 不会影响失敏状态下的受体结构或结构域排列。因此,我们的研究首次详细描述了 GluK1-1a 受体的结构和功能特征,强调了剪接插入在调节受体特性及其调节中的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/753c/11540303/54d514e15cb0/elife-89755-fig1.jpg

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