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Structure paper

TitleMechanisms underlying TARP modulation of the GluA1/2-γ8 AMPA receptor.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 734, Year 2022
Publish dateFeb 8, 2022
AuthorsBeatriz Herguedas / Bianka K Kohegyi / Jan-Niklas Dohrke / Jake F Watson / Danyang Zhang / Hinze Ho / Saher A Shaikh / Remigijus Lape / James M Krieger / Ingo H Greger /
PubMed AbstractAMPA-type glutamate receptors (AMPARs) mediate rapid signal transmission at excitatory synapses in the brain. Glutamate binding to the receptor's ligand-binding domains (LBDs) leads to ion channel ...AMPA-type glutamate receptors (AMPARs) mediate rapid signal transmission at excitatory synapses in the brain. Glutamate binding to the receptor's ligand-binding domains (LBDs) leads to ion channel activation and desensitization. Gating kinetics shape synaptic transmission and are strongly modulated by transmembrane AMPAR regulatory proteins (TARPs) through currently incompletely resolved mechanisms. Here, electron cryo-microscopy structures of the GluA1/2 TARP-γ8 complex, in both open and desensitized states (at 3.5 Å), reveal state-selective engagement of the LBDs by the large TARP-γ8 loop ('β1'), elucidating how this TARP stabilizes specific gating states. We further show how TARPs alter channel rectification, by interacting with the pore helix of the selectivity filter. Lastly, we reveal that the Q/R-editing site couples the channel constriction at the filter entrance to the gate, and forms the major cation binding site in the conduction path. Our results provide a mechanistic framework of how TARPs modulate AMPAR gating and conductance.
External linksNat Commun / PubMed:35136046 / PubMed Central
MethodsEM (single particle)
Resolution3.39 - 4.78 Å
Structure data

13969

7qhb

EMDB-13969, PDB-7qhb:
Active state of GluA1/2 in complex with TARP gamma 8, L-glutamate and CTZ
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-13970:
Active state of GluA1/A2 AMPA receptor in complex with TARP gamma-8 (TMD)
Method: EM (single particle) / Resolution: 3.39 Å

EMDB-13971:
Active state of GluA1/A2 AMPA receptor in complex with TARP gamma-8 (LBD)
Method: EM (single particle) / Resolution: 3.6 Å

13972

7qhh

EMDB-13972, PDB-7qhh:
Desensitized state of GluA1/2 AMPA receptor in complex with TARP-gamma 8 (TMD-LBD)
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-13973:
Desensitized state of GluA1/2 AMPA receptor in complex with TARP-gamma 8 (TMD)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-13974:
Desensitized state of GluA1/2 AMPA receptor in complex with TARP-gamma 8 (LBD)
Method: EM (single particle) / Resolution: 4.78 Å

Chemicals

ChemComp-PAM:
PALMITOLEIC ACID / Palmitoleic acid

ChemComp-GLU:
GLUTAMIC ACID / Glutamic acid

ChemComp-CYZ:
CYCLOTHIAZIDE / Cyclothiazide

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-79N:
(2S)-2,3-dihydroxypropyl (7Z)-hexadec-7-enoate

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / glutamate / AMPA receptor / TARPs

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