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

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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2013-01, Vol.110 (2), p.725-730
Main Authors: Budreck, Elaine C., Kwon, Oh-Bin, Jung, Jung Hoon, Baudouin, Stephane, Thommen, Albert, Kim, Hye-Sun, Fukazawa, Yugo, Harada, Harumi, Tabuchi, Katsuhiko, Shigemoto, Ryuichi, Scheiffele, Peter, Kim, Joung-Hun
Format: Article
Language:English
Subjects:
Analysis of Variance
Animals
Antibodies
Behavioral neuroscience
Biochemistry
Biological and medical sciences
Biological Sciences
Blotting, Western
cell adhesion
Cell adhesion & migration
Cell Adhesion Molecules, Neuronal - metabolism
Dizocilpine Maleate
Fundamental and applied biological sciences. Psychology
glutamic acid
Immunoprecipitation
Long term potentiation
Microscopy, Confocal
Microscopy, Immunoelectron
Molecular biology
N methyl D aspartate receptors
Neurochemistry
Neuronal Plasticity - physiology
Neurons
Neurotransmitters
Protein isoforms
Proteins
Rats
Receptors
Receptors, Ionotropic Glutamate - metabolism
Receptors, N-Methyl-D-Aspartate - metabolism
Statistics, Nonparametric
Synapses
Synapses - physiology
Synaptic transmission
Synaptic Transmission - physiology
Vertebrates: nervous system and sense organs
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1214718110