Structure and organization of heteromeric AMPA-type glutamate receptors-Reference-Cited by-同舟云学术

Structure and organization of heteromeric AMPA-type glutamate receptors

Published:2016-04-29 Issue:6285 Volume:352 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Herguedas Beatriz¹,García-Nafría Javier¹,Cais Ondrej¹,Fernández-Leiro Rafael²,Krieger James¹,Ho Hinze¹,Greger Ingo H.¹

Affiliation:

1. Neurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.

2. Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, UK.

Abstract

Signaling at the synapse Neurons signal to each other at synapses using neurotransmitters. Glutamate is a key neurotransmitter, and AMPA-type glutamate receptors (AMPARs) mediate rapid responses to glutamate release. These receptors mainly occur as heteromers comprising GluA1-4 subunits. Herguedas et al. used electron microscopy and x-ray crystallography to determine the structure of GluA2/3 and GluA2/4 heteromers. The structures differ from those determined previously for GluA2 homomers but emphasize how signals may be transmitted through these dynamic receptors. Science , this issue p. 10.1126/science.aad3873

Funder

Medical Research Council

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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