Cdk5-dependent phosphorylation of liprinα1 mediates neuronal activity-dependent synapse development
The experience-dependent modulation of brain circuitry depends on dynamic changes in synaptic connections that are guided by neuronal activity. In particular, postsynaptic maturation requires changes in dendritic spine morphology, the targeting of postsynaptic proteins, and the insertion of synaptic...
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| Autor*in: |
Huiqian Huang [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 114(2017), 33, Seite E6992 |
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| Übergeordnetes Werk: |
volume:114 ; year:2017 ; number:33 ; pages:E6992 |
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| 520 | |a The experience-dependent modulation of brain circuitry depends on dynamic changes in synaptic connections that are guided by neuronal activity. In particular, postsynaptic maturation requires changes in dendritic spine morphology, the targeting of postsynaptic proteins, and the insertion of synaptic neurotransmitter receptors. Thus, it is critical to understand how neuronal activity controls postsynaptic maturation. Here we report that the scaffold protein liprina1 and its phosphorylation by cyclin-dependent kinase 5 (Cdk5) are critical for the maturation of excitatory synapses through regulation of the synaptic localization of the major postsynaptic organizer postsynaptic density (PSD)-95. Whereas Cdk5 phosphorylates liprina1 at Thr701, this phosphorylation decreases in neurons in response to neuronal activity. Blockade of liprina1 phosphorylation enhances the structural and functional maturation of excitatory synapses. Nanoscale superresolution imaging reveals that inhibition of liprina1 phosphorylation increases the colocalization of liprina1 with PSD-95. Furthermore, disruption of liprina1 phosphorylation by a small interfering peptide, siLIP, promotes the synaptic localization of PSD-95 and enhances synaptic strength in vivo. Our findings collectively demonstrate that the Cdk5-dependent phosphorylation of liprina1 is important for the postsynaptic organization during activity-dependent synapse development. | ||
| 650 | 4 | |a Synaptic strength | |
| 650 | 4 | |a Dendritic spines | |
| 650 | 4 | |a Synapses | |
| 650 | 4 | |a Neuroimaging | |
| 650 | 4 | |a Postsynaptic density proteins | |
| 650 | 4 | |a Receptors | |
| 650 | 4 | |a Brain | |
| 650 | 4 | |a Circuits | |
| 650 | 4 | |a Disruption | |
| 650 | 4 | |a Localization | |
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| 650 | 4 | |a Cyclin-dependent kinase 5 | |
| 650 | 4 | |a Maturation | |
| 650 | 4 | |a Spine | |
| 650 | 4 | |a Phosphorylation | |
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| 650 | 4 | |a Structure-function relationships | |
| 650 | 4 | |a Neurotransmitter receptors | |
| 650 | 4 | |a Neurons | |
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a Postsynaptic density | |
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| 700 | 0 | |a Teng Zhao |4 oth | |
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| 700 | 0 | |a Michael M T Loy |4 oth | |
| 700 | 0 | |a Kwok-On Lai |4 oth | |
| 700 | 0 | |a Amy K Y Fu |4 oth | |
| 700 | 0 | |a Nancy Y Ip |4 oth | |
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cdk5-dependent phosphorylation of liprinα1 mediates neuronal activity-dependent synapse development |
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Cdk5-dependent phosphorylation of liprinα1 mediates neuronal activity-dependent synapse development |
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The experience-dependent modulation of brain circuitry depends on dynamic changes in synaptic connections that are guided by neuronal activity. In particular, postsynaptic maturation requires changes in dendritic spine morphology, the targeting of postsynaptic proteins, and the insertion of synaptic neurotransmitter receptors. Thus, it is critical to understand how neuronal activity controls postsynaptic maturation. Here we report that the scaffold protein liprina1 and its phosphorylation by cyclin-dependent kinase 5 (Cdk5) are critical for the maturation of excitatory synapses through regulation of the synaptic localization of the major postsynaptic organizer postsynaptic density (PSD)-95. Whereas Cdk5 phosphorylates liprina1 at Thr701, this phosphorylation decreases in neurons in response to neuronal activity. Blockade of liprina1 phosphorylation enhances the structural and functional maturation of excitatory synapses. Nanoscale superresolution imaging reveals that inhibition of liprina1 phosphorylation increases the colocalization of liprina1 with PSD-95. Furthermore, disruption of liprina1 phosphorylation by a small interfering peptide, siLIP, promotes the synaptic localization of PSD-95 and enhances synaptic strength in vivo. Our findings collectively demonstrate that the Cdk5-dependent phosphorylation of liprina1 is important for the postsynaptic organization during activity-dependent synapse development. |
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The experience-dependent modulation of brain circuitry depends on dynamic changes in synaptic connections that are guided by neuronal activity. In particular, postsynaptic maturation requires changes in dendritic spine morphology, the targeting of postsynaptic proteins, and the insertion of synaptic neurotransmitter receptors. Thus, it is critical to understand how neuronal activity controls postsynaptic maturation. Here we report that the scaffold protein liprina1 and its phosphorylation by cyclin-dependent kinase 5 (Cdk5) are critical for the maturation of excitatory synapses through regulation of the synaptic localization of the major postsynaptic organizer postsynaptic density (PSD)-95. Whereas Cdk5 phosphorylates liprina1 at Thr701, this phosphorylation decreases in neurons in response to neuronal activity. Blockade of liprina1 phosphorylation enhances the structural and functional maturation of excitatory synapses. Nanoscale superresolution imaging reveals that inhibition of liprina1 phosphorylation increases the colocalization of liprina1 with PSD-95. Furthermore, disruption of liprina1 phosphorylation by a small interfering peptide, siLIP, promotes the synaptic localization of PSD-95 and enhances synaptic strength in vivo. Our findings collectively demonstrate that the Cdk5-dependent phosphorylation of liprina1 is important for the postsynaptic organization during activity-dependent synapse development. |
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The experience-dependent modulation of brain circuitry depends on dynamic changes in synaptic connections that are guided by neuronal activity. In particular, postsynaptic maturation requires changes in dendritic spine morphology, the targeting of postsynaptic proteins, and the insertion of synaptic neurotransmitter receptors. Thus, it is critical to understand how neuronal activity controls postsynaptic maturation. Here we report that the scaffold protein liprina1 and its phosphorylation by cyclin-dependent kinase 5 (Cdk5) are critical for the maturation of excitatory synapses through regulation of the synaptic localization of the major postsynaptic organizer postsynaptic density (PSD)-95. Whereas Cdk5 phosphorylates liprina1 at Thr701, this phosphorylation decreases in neurons in response to neuronal activity. Blockade of liprina1 phosphorylation enhances the structural and functional maturation of excitatory synapses. Nanoscale superresolution imaging reveals that inhibition of liprina1 phosphorylation increases the colocalization of liprina1 with PSD-95. Furthermore, disruption of liprina1 phosphorylation by a small interfering peptide, siLIP, promotes the synaptic localization of PSD-95 and enhances synaptic strength in vivo. Our findings collectively demonstrate that the Cdk5-dependent phosphorylation of liprina1 is important for the postsynaptic organization during activity-dependent synapse development. |
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