Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization
Autor: | Daniel T.S. Pak, Zikai Zhou, Yuehua Zhu, Guiqin He, Wei Xie, Zhengping Jia, Rui Dang, Celeste Leung, Junxia Qi, An Liu |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Dendritic spine Cell Adhesion Molecules Neuronal Dendritic Spines Neurexin Neuroligin macromolecular substances Biology Hippocampus Article Synapse 03 medical and health sciences 0302 clinical medicine Postsynaptic potential Animals Humans Research Articles Cerebral Cortex Neuronal Plasticity Lim Kinases Cell Biology Cofilin Actin cytoskeleton 3. Good health Cell biology Actin Cytoskeleton 030104 developmental biology Actin Depolymerizing Factors Synapses Synaptic plasticity 030217 neurology & neurosurgery |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
DOI: | 10.1083/jcb.201509023 |
Popis: | The C-terminal domain of NLG1 is sufficient to enhance spine and synapse number and to modulate synaptic plasticity, and it exerts these effects via its interaction with SPAR and the subsequent activation of 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. |
Databáze: | OpenAIRE |
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