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Structure paper

TitleGating and modulation of a hetero-octameric AMPA glutamate receptor.
Journal, issue, pagesNature, Vol. 594, Issue 7863, Page 454-458, Year 2021
Publish dateJun 2, 2021
AuthorsDanyang Zhang / Jake F Watson / Peter M Matthews / Ondrej Cais / Ingo H Greger /
PubMed AbstractAMPA receptors (AMPARs) mediate the majority of excitatory transmission in the brain and enable the synaptic plasticity that underlies learning. A diverse array of AMPAR signalling complexes are ...AMPA receptors (AMPARs) mediate the majority of excitatory transmission in the brain and enable the synaptic plasticity that underlies learning. A diverse array of AMPAR signalling complexes are established by receptor auxiliary subunits, which associate with the AMPAR in various combinations to modulate trafficking, gating and synaptic strength. However, their mechanisms of action are poorly understood. Here we determine cryo-electron microscopy structures of the heteromeric GluA1-GluA2 receptor assembled with both TARP-γ8 and CNIH2, the predominant AMPAR complex in the forebrain, in both resting and active states. Two TARP-γ8 and two CNIH2 subunits insert at distinct sites beneath the ligand-binding domains of the receptor, with site-specific lipids shaping each interaction and affecting the gating regulation of the AMPARs. Activation of the receptor leads to asymmetry between GluA1 and GluA2 along the ion conduction path and an outward expansion of the channel triggers counter-rotations of both auxiliary subunit pairs, promoting the active-state conformation. In addition, both TARP-γ8 and CNIH2 pivot towards the pore exit upon activation, extending their reach for cytoplasmic receptor elements. CNIH2 achieves this through its uniquely extended M2 helix, which has transformed this endoplasmic reticulum-export factor into a powerful AMPAR modulator that is capable of providing hippocampal pyramidal neurons with their integrative synaptic properties.
External linksNature / PubMed:34079129 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.6 Å
Structure data

EMDB-12802, PDB-7oca:
Resting state full-length GluA1/A2 heterotertramer in complex with TARP gamma 8 and CNIH2
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-12803, PDB-7occ:
NTD of resting state GluA1/A2 heterotertramer
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-12804, PDB-7ocd:
Resting state GluA1/A2 heterotetramer in complex with auxiliary subunit TARP gamma 8 (LBD-TMD)
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-12805, PDB-7oce:
Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-12806, PDB-7ocf:
Active state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD)
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-E2Q:
6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide / antagonist*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-CLR:
CHOLESTEROL

ChemComp-CYZ:
CYCLOTHIAZIDE

ChemComp-GLU:
GLUTAMIC ACID

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / AMPAR / ion channels / neurotransmission

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