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• W2025704881 abstract "AMPA-type glutamate receptors (AMPARs) mediate fast neurotransmission at excitatory synapses. The extent and fidelity of postsynaptic depolarization triggered by AMPAR activation are shaped by AMPAR auxiliary subunits, including the transmembrane AMPAR regulatory proteins (TARPs). TARPs profoundly influence gating, an effect thought to be mediated by an interaction with the AMPAR ion channel and ligand binding domain (LBD). Here, we show that the distal N-terminal domain (NTD) contributes to TARP modulation. Alterations in the NTD-LBD linker result in TARP-dependent and TARP-selective changes in AMPAR gating. Using peptide arrays, we identify a TARP interaction region on the NTD and define the path of TARP contacts along the LBD surface. Moreover, we map key binding sites on the TARP itself and show that mutation of these residues mediates gating modulation. Our data reveal a TARP-dependent allosteric role for the AMPAR NTD and suggest that TARP binding triggers a drastic reorganization of the AMPAR complex." @default.
• W2025704881 created "2016-06-24" @default.
• W2025704881 creator A5031041004 @default.
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• W2025704881 creator A5069305015 @default.
• W2025704881 creator A5076267142 @default.
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• W2025704881 date "2014-10-01" @default.
• W2025704881 modified "2023-10-01" @default.
• W2025704881 title "Mapping the Interaction Sites between AMPA Receptors and TARPs Reveals a Role for the Receptor N-Terminal Domain in Channel Gating" @default.
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• W2025704881 doi "https://doi.org/10.1016/j.celrep.2014.09.029" @default.
• W2025704881 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4405707" @default.
• W2025704881 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25373908" @default.
• W2025704881 hasPublicationYear "2014" @default.
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