Neuroligin-1 controls synaptic abundance of NMDA-type glutamate receptors through extracellular coupling

被引：139

作者：

Budreck, Elaine C. ^{[1
]}

Kwon, Oh-Bin ^{[2
]}

Jung, Jung Hoon ^{[2
]}

Baudouin, Stephane ^{[1
]}

Thommen, Albert ^{[1
]}

Kim, Hye-Sun ^{[3
]}

Fukazawa, Yugo ^{[4
,5
]}

Harada, Harumi ^{[4
,5
]}

Tabuchi, Katsuhiko ^{[4
,5
,6
]}

Shigemoto, Ryuichi ^{[4
,5
,7
]}

Scheiffele, Peter ^{[1
]}

Kim, Joung-Hun ^{[2
]}

机构：

[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland

[2] Pohang Univ Sci & Technol POSTECH, Dept Life Sci, Pohang 790784, Gyungbuk, South Korea

[3] Seoul Natl Univ, Coll Med, Dept Pharmacol, Seoul 110799, South Korea

[4] Natl Inst Physiol Sci, Div Cerebral Struct, Okazaki, Aichi 4448787, Japan

[5] Grad Univ Adv Studies, Dept Physiol Sci, Okazaki, Aichi 4448787, Japan

[6] Japan Sci & Technol Agcy, Precursory Res Embryon Sci & Technol PRESTO, Kawaguchi, Saitama 3320012, Japan

[7] Japan Sci & Technol Agcy, SORST, Kawaguchi, Saitama 3330012, Japan

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2013年 / 110卷 / 02期

基金：

瑞士国家科学基金会; 美国国家卫生研究院; 新加坡国家研究基金会;

关键词：

synapse; neurotranmitter receptor; neurexin; CELL-ADHESION MOLECULE; INHIBITORY SYNAPSES; AMPA RECEPTORS; TRAFFICKING; PLASTICITY; PROTEIN; PSD-95; EXPRESSION; MATURATION; SUBUNITS;

D O I：

10.1073/pnas.1214718110

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Despite the pivotal functions of the NMDA receptor (NMDAR) for neural circuit development and synaptic plasticity, the molecular mechanisms underlying the dynamics of NMDAR trafficking are poorly understood. The cell adhesion molecule neuroligin-1 (NL1) modifies NMDAR-dependent synaptic transmission and synaptic plasticity, but it is unclear whether NL1 controls synaptic accumulation or function of the receptors. Here, we provide evidence that NL1 regulates the abundance of NMDARs at postsynaptic sites. This function relies on extracellular, NL1 isoform-specific sequences that facilitate biochemical interactions between NL1 and the NMDAR GluN1 subunit. Our work uncovers NL1 isoform-specific cis-interactions with ionotropic glutamate receptors as a key mechanism for controlling synaptic properties.

引用

页码：725 / 730

页数：6

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