Structure of transmembrane AMPA receptor regulatory protein subunit γ2

IF 15.7 1区综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES

Nature Communications Pub Date : 2025-01-15 DOI:10.1038/s41467-025-56027-1

W. Dylan Hale, Alejandra Montaño Romero, Nicholas Koylass, Collin R. Warrick, Zhaozhu Qiu, Richard L. Huganir, Edward C. Twomey

引用次数: 0

Abstract

Transmembrane AMPA receptor regulatory proteins (TARPs) are claudin-like proteins that tightly regulate AMPA receptors (AMPARs) and are fundamental for excitatory neurotransmission. With cryo-electron microscopy (cryo-EM) we reconstruct the 36 kDa TARP subunit γ2 to 2.3 Å, which points to structural diversity among TARPs. Our data reveals critical motifs that distinguish TARPs from claudins and define how sequence variations within TARPs differentiate subfamilies and their regulation of AMPARs.

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跨膜AMPA受体调节蛋白亚基γ - 2的结构

跨膜AMPA受体调节蛋白（TARPs）是一种紧密调节AMPA受体（AMPARs）的cladin样蛋白，是兴奋性神经传递的基础。利用低温电镜（cryo-EM）重建了36 kDa的TARP亚基γ2至2.3 Å，这表明了TARPs之间的结构多样性。我们的数据揭示了区分TARPs和cladin的关键基序，并定义了TARPs内的序列变化如何区分亚家族及其对ampar的调节。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Nature Communications Biological Science Disciplines-

CiteScore

24.90

自引率

2.40%

发文量

6928

审稿时长

3.7 months

期刊介绍： Nature Communications, an open-access journal, publishes high-quality research spanning all areas of the natural sciences. Papers featured in the journal showcase significant advances relevant to specialists in each respective field. With a 2-year impact factor of 16.6 (2022) and a median time of 8 days from submission to the first editorial decision, Nature Communications is committed to rapid dissemination of research findings. As a multidisciplinary journal, it welcomes contributions from biological, health, physical, chemical, Earth, social, mathematical, applied, and engineering sciences, aiming to highlight important breakthroughs within each domain.