质子如何塑造 AMPA 受体的结构、功能和在突触中的扩散

IF 12.5 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Nature Structural & Molecular Biology Pub Date : 2024-08-13 DOI:10.1038/s41594-024-01371-x
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引用次数: 0

摘要

细胞外 AMPA 受体 N 端结构域(NTD)通过调整受体扩散影响突触强度。我们揭示了伴随突触活动的 pH 波动通过 NTD 组氨酸残基的质子感应改变了功能上占主导地位的 GluA2 亚基的 NTD 构象,从而增加了门控动力学和受体在突触处的扩散。
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How protons shape AMPA receptor structure, function and diffusion at the synapse
The extracellular AMPA receptor N-terminal domain (NTD) affects synaptic strength by tuning receptor diffusion. We reveal that pH fluctuations accompanying synaptic activity alter NTD conformation of the functionally dominant GluA2 subunit, via proton sensing by an NTD histidine residue, thereby increasing gating kinetics and receptor diffusion at the synapse.
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来源期刊
Nature Structural & Molecular Biology
Nature Structural & Molecular Biology BIOCHEMISTRY & MOLECULAR BIOLOGY-BIOPHYSICS
CiteScore
22.00
自引率
1.80%
发文量
160
审稿时长
3-8 weeks
期刊介绍: Nature Structural & Molecular Biology is a comprehensive platform that combines structural and molecular research. Our journal focuses on exploring the functional and mechanistic aspects of biological processes, emphasizing how molecular components collaborate to achieve a particular function. While structural data can shed light on these insights, our publication does not require them as a prerequisite.
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