Structure of transmembrane AMPA receptor regulatory protein subunit γ2
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 s...
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Nature Portfolio
2025-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-025-56027-1 |
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author | W. Dylan Hale Alejandra Montaño Romero Nicholas Koylass Collin R. Warrick Zhaozhu Qiu Richard L. Huganir Edward C. Twomey |
author_facet | W. Dylan Hale Alejandra Montaño Romero Nicholas Koylass Collin R. Warrick Zhaozhu Qiu Richard L. Huganir Edward C. Twomey |
author_sort | W. Dylan Hale |
collection | DOAJ |
description | 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. |
format | Article |
id | doaj-art-d05d36bd3b7f404f8c75c931055ae4ae |
institution | Kabale University |
issn | 2041-1723 |
language | English |
publishDate | 2025-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj-art-d05d36bd3b7f404f8c75c931055ae4ae2025-01-19T12:31:49ZengNature PortfolioNature Communications2041-17232025-01-011611710.1038/s41467-025-56027-1Structure of transmembrane AMPA receptor regulatory protein subunit γ2W. Dylan Hale0Alejandra Montaño Romero1Nicholas Koylass2Collin R. Warrick3Zhaozhu Qiu4Richard L. Huganir5Edward C. Twomey6Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of MedicineSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of MedicineDepartment of Physiology, Johns Hopkins University School of MedicineSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of MedicineSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of MedicineSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of MedicineSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of MedicineAbstract 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.https://doi.org/10.1038/s41467-025-56027-1 |
spellingShingle | W. Dylan Hale Alejandra Montaño Romero Nicholas Koylass Collin R. Warrick Zhaozhu Qiu Richard L. Huganir Edward C. Twomey Structure of transmembrane AMPA receptor regulatory protein subunit γ2 Nature Communications |
title | Structure of transmembrane AMPA receptor regulatory protein subunit γ2 |
title_full | Structure of transmembrane AMPA receptor regulatory protein subunit γ2 |
title_fullStr | Structure of transmembrane AMPA receptor regulatory protein subunit γ2 |
title_full_unstemmed | Structure of transmembrane AMPA receptor regulatory protein subunit γ2 |
title_short | Structure of transmembrane AMPA receptor regulatory protein subunit γ2 |
title_sort | structure of transmembrane ampa receptor regulatory protein subunit γ2 |
url | https://doi.org/10.1038/s41467-025-56027-1 |
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