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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Main Authors: W. Dylan Hale, Alejandra Montaño Romero, Nicholas Koylass, Collin R. Warrick, Zhaozhu Qiu, Richard L. Huganir, Edward C. Twomey
Format: Article
Language:English
Published: Nature Portfolio 2025-01-01
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.
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publishDate 2025-01-01
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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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