Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization
Copyright policy )Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization
Neuroligin (NLG) 1 is important for synapse development and function, but the underlying mechanisms remain unclear. It is known that at least some aspects of NLG1 function are independent of the presynaptic neurexin, suggesting that the C-terminal domain (CTD) of NLG1 may be sufficient for synaptic regulation. In addition, NLG1 is subjected to activity-dependent proteolytic cleavage, generating a cytosolic CTD fragment, but the significance of this process remains unknown. In this study, we show that the CTD of NLG1 is sufficient to (a) enhance spine and synapse number, (b) modulate synaptic plasticity, and (c) exert these effects via its interaction with spine-associated Rap guanosine triphosphatase–activating protein and subsequent activation of LIM-domain protein kinase 1/cofilin–mediated actin reorganization. Our results provide a novel postsynaptic mechanism by which NLG1 regulates synapse development and function.
- University of Washington Medical Center United States
- Southeast University China (People's Republic of)
- University of Toronto Canada
- Southwest University China (People's Republic of)
- Hospital for Sick Children Canada
Cerebral Cortex, Mice, Knockout, Neuronal Plasticity, Genotype, Cell Adhesion Molecules, Neuronal, Dendritic Spines, GTPase-Activating Proteins, Lim Kinases, In Vitro Techniques, Hippocampus, Actin Cytoskeleton, HEK293 Cells, Phenotype, Actin Depolymerizing Factors, Animals, Humans, Protein Interaction Domains and Motifs, RNA Interference, Phosphorylation, Research Articles, Protein Binding
Cerebral Cortex, Mice, Knockout, Neuronal Plasticity, Genotype, Cell Adhesion Molecules, Neuronal, Dendritic Spines, GTPase-Activating Proteins, Lim Kinases, In Vitro Techniques, Hippocampus, Actin Cytoskeleton, HEK293 Cells, Phenotype, Actin Depolymerizing Factors, Animals, Humans, Protein Interaction Domains and Motifs, RNA Interference, Phosphorylation, Research Articles, Protein Binding
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