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Structure of Transmembrane AMPA Receptor Regulatory Protein Subunit γ2
Open accessPreprint — published as 10.1038/s41467-025-56027-1
Abstract
Transmembrane AMPA receptor regulatory proteins (TARPs) are claudin-like proteins that tightly regulate AMPA receptors (AMPARs) and are fundamental for excitatory neurotransmission. We used cryo-electron microscopy (cryo-EM) to reconstruct the 36 kDa TARP subunit γ2 to 2.3 Å and reveal the structural diversity of 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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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Hale, W. D., Romero, A. M., Huganir, R. L., & Twomey, E. C.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Huganir, Richard L.
- Twomey, Edward C.
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2023-11-28
- Volume
- 16
- Issue
- 1
- Pages
- 671-671
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11733119
- OpenAlex
- W4406361254
- Cited by
- 8
- References
- 1
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 1
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Nature Communications (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Health and Human Services (RF1NS134549, K99MH132811, R35GM154904, R01 NS118014, R35 GM124824, R01NS036715)
- Kinship Foundation (22098168)
- Johns Hopkins University
- Diana Helis Henry Medical Research Foundation (142548)
- Searle Scholars Program (22098168)
- National Institutes of Health (NS036715)
- National Institute of Mental Health (K99MH132811, R01MH112152)
- National Institute of General Medical Sciences (R35GM154904, R35GM124824)
- National Institute of Neurological Disorders and Stroke (R01NS036715, RF1NS134549, R01NS118014, R37NS036715)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Keywords
- transmembrane AMPA receptor regulatory proteins, tetraspanins, glutamate receptors, excitatory neurotransmission, cryo-EM structure
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