Crystal structure and association behaviour of the GluR2 amino-terminal domain

Rongsheng Jin; Satinder K. Singh; Shenyan Gu; Hiroyasu Furukawa; Alexander I. Sobolevsky; Jie Zhou; Yan Jin; Eric Gouaux

doi:10.1038/emboj.2009.140

Crystal structure and association behaviour of the GluR2 amino-terminal domain

Rongsheng Jin, Satinder K. Singh, Shenyan Gu, Hiroyasu Furukawa, Alexander I. Sobolevsky, Jie Zhou, Yan Jin, Eric Gouaux

Research output: Contribution to journal › Article › peer-review

133 Scopus citations

Abstract

Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.

Original language	English (US)
Pages (from-to)	1812-1823
Number of pages	12
Journal	EMBO Journal
Volume	28
Issue number	12
DOIs	https://doi.org/10.1038/emboj.2009.140
State	Published - Jun 17 2009
Externally published	Yes

Keywords

Amino-terminal domain
GluR2
Glutamate receptor
Ion channel
X-ray crystallography

ASJC Scopus subject areas

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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10.1038/emboj.2009.140

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title = "Crystal structure and association behaviour of the GluR2 amino-terminal domain",

abstract = "Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.",

keywords = "Amino-terminal domain, GluR2, Glutamate receptor, Ion channel, X-ray crystallography",

author = "Rongsheng Jin and Singh, {Satinder K.} and Shenyan Gu and Hiroyasu Furukawa and Sobolevsky, {Alexander I.} and Jie Zhou and Yan Jin and Eric Gouaux",

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month = jun,

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AU - Jin, Rongsheng

AU - Singh, Satinder K.

AU - Gu, Shenyan

AU - Furukawa, Hiroyasu

AU - Sobolevsky, Alexander I.

AU - Zhou, Jie

AU - Jin, Yan

AU - Gouaux, Eric

PY - 2009/6/17

Y1 - 2009/6/17

N2 - Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.

AB - Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.

KW - Amino-terminal domain

KW - GluR2

KW - Glutamate receptor

KW - Ion channel

KW - X-ray crystallography

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Crystal structure and association behaviour of the GluR2 amino-terminal domain

Abstract

Keywords

ASJC Scopus subject areas

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