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- W2082689075 abstract "Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that play critical roles in excitatory neurotransmission. A functional iGluR is composed of four subunits, each containing an amino-terminal domain (ATD), a ligand-binding domain (LBD), a transmembrane domain (TMD) composed of three transmembrane helices (M1, M3 and M4) and a re-entrant loop (M2), as well as an intracellular carboxyl-terminal domain (CTD). Formation of the tetrameric complex, which is a prerequisite for the receptor's surface expression and function, involves a dimeric intermediate. Nevertheless, the biophysical mechanisms underlying iGluR oligomerization remain largely unknown. We studied the relative energetic contributions of the different structural domains to the oligomerization of iGluRs using blue native PAGE and fluorescent size-exclusion chromatography (FSEC). We find that deletion of the M4 transmembrane helix renders AMPA receptors incapable of tetramerization and traps them in a dimeric form, suggesting that the crucial dimer-to-tetramer transition is driven by molecular interactions within the TMD. Further highlighting the importance of TMD to AMPA receptor tetramerization, the isolated TMD of the GluA1 subunit, which lacks ATD and LBD, still form tetramers. On the other hand, the GluA1 ATD is essential for the stability of homo-dimer intermediates, although its absence does not prevent tetramerization. Interestingly, the prokaryotic glutamate receptor GluR0, which lacks both the ATD and the M4 helix, forms both dimers and functional tetramers. In contrast, GluA1 subunits lacking the ATD and the M4 helix (and thus topologically similar to GluR0) do not oligomerize, forming monomers only. Our results indicate that the mechanisms for tetrameric assembly differ significantly between GluA1 and GluR0 in terms of the energetic contributions of each structural domain. Such differences may have important implications in the evolution of iGluRs and their roles in fast excitatory neurotransmission." @default.
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- W2082689075 date "2013-01-01" @default.
- W2082689075 modified "2023-09-28" @default.
- W2082689075 title "Structural Mechanisms underlying AMPA Receptor Oligomerization" @default.
- W2082689075 doi "https://doi.org/10.1016/j.bpj.2012.11.1537" @default.
- W2082689075 hasPublicationYear "2013" @default.
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