Structure and mechanism of AMPA receptor - auxiliary protein complexes.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
02 2019
02 2019
Historique:
received:
09
01
2019
revised:
25
01
2019
accepted:
28
01
2019
pubmed:
3
3
2019
medline:
18
2
2020
entrez:
3
3
2019
Statut:
ppublish
Résumé
Ionotropic glutamate receptors in vertebrates are composed of three major subtypes - AMPA, kainate, and NMDA receptors - and mediate the majority of fast excitatory neurotransmission at chemical synapses of the central nervous system. Among the three major families, native AMPA receptors function as complexes with a variety of auxiliary subunits, which in turn modulate receptor trafficking, gating, pharmacology, and permeation. Despite the long history of structure-mechanism studies using soluble receptor domains or intact yet isolated receptors, structures of AMPA receptor-auxiliary subunit complexes have not been available until recent breakthroughs in single-particle cryo-electron microscopy. Single particle cryo-EM studies have, in turn, provided new insights into the structure and organization of AMPA receptor - auxiliary protein complexes and into the molecular mechanisms of AMPA receptor activation and desensitization.
Identifiants
pubmed: 30825796
pii: S0959-440X(19)30009-0
doi: 10.1016/j.sbi.2019.01.011
pmc: PMC6592759
mid: NIHMS1520884
pii:
doi:
Substances chimiques
Protein Subunits
0
Receptors, AMPA
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
104-111Subventions
Organisme : NINDS NIH HHS
ID : R01 NS038631
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.
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