Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 104-111 |
| Number of pages | 8 |
| Journal | Current Opinion in Structural Biology |
| Volume | 54 |
| DOIs | |
| State | Published - Feb 1 2019 |
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ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
Cite this
Structure and mechanism of AMPA receptor — auxiliary protein complexes. / Chen, Shanshuang; Gouaux, Eric.
In: Current Opinion in Structural Biology, Vol. 54, 01.02.2019, p. 104-111.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Structure and mechanism of AMPA receptor — auxiliary protein complexes
AU - Chen, Shanshuang
AU - Gouaux, Eric
PY - 2019/2/1
Y1 - 2019/2/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=85062023623&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2019.01.011
DO - 10.1016/j.sbi.2019.01.011
M3 - Review article
C2 - 30825796
AN - SCOPUS:85062023623
VL - 54
SP - 104
EP - 111
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
SN - 0959-440X
ER -