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Requirement for Protein Synthesis at Developing Synapses
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| Zeitschriftentitel: | The Journal of Neuroscience |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | The Journal of Neuroscience, 29, 2009, 31, S. 9778-9793 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Society for Neuroscience
|
| Schlagwörter: |
| author_facet |
Sebeo, Joseph Hsiao, Kuangfu Bozdagi, Ozlem Dumitriu, Dani Ge, Yongchao Zhou, Qiang Benson, Deanna L. Sebeo, Joseph Hsiao, Kuangfu Bozdagi, Ozlem Dumitriu, Dani Ge, Yongchao Zhou, Qiang Benson, Deanna L. |
|---|---|
| author |
Sebeo, Joseph Hsiao, Kuangfu Bozdagi, Ozlem Dumitriu, Dani Ge, Yongchao Zhou, Qiang Benson, Deanna L. |
| spellingShingle |
Sebeo, Joseph Hsiao, Kuangfu Bozdagi, Ozlem Dumitriu, Dani Ge, Yongchao Zhou, Qiang Benson, Deanna L. The Journal of Neuroscience Requirement for Protein Synthesis at Developing Synapses General Neuroscience |
| author_sort |
sebeo, joseph |
| spelling |
Sebeo, Joseph Hsiao, Kuangfu Bozdagi, Ozlem Dumitriu, Dani Ge, Yongchao Zhou, Qiang Benson, Deanna L. 0270-6474 1529-2401 Society for Neuroscience General Neuroscience http://dx.doi.org/10.1523/jneurosci.2613-09.2009 <jats:p>Activity and protein synthesis act cooperatively to generate persistent changes in synaptic responses. This forms the basis for enduring memory in adults. Activity also shapes neural circuits developmentally, but whether protein synthesis plays a congruent function in this process is poorly understood. Here, we show that brief periods of global or local protein synthesis inhibition decrease the synaptic vesicles available for fusion and increase synapse elimination. Ca<jats:sup>2+</jats:sup>/calmodulin-dependent protein kinase II (CaMKII) is a critical target; its levels are controlled by rapid turnover, and blocking its activity or knocking it down recapitulates the effects of protein synthesis inhibition. Mature presynaptic terminals show decreased sensitivity to protein synthesis inhibition, and resistance coincides with a developmental switch in regulation from CaMKII to PKA (protein kinase A). These findings demonstrate a novel mechanism regulating presynaptic activity and synapse elimination during development, and suggest that protein translation acts coordinately with activity to selectively stabilize appropriate synaptic interactions.</jats:p> Requirement for Protein Synthesis at Developing Synapses The Journal of Neuroscience |
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| title |
Requirement for Protein Synthesis at Developing Synapses |
| title_unstemmed |
Requirement for Protein Synthesis at Developing Synapses |
| title_full |
Requirement for Protein Synthesis at Developing Synapses |
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Requirement for Protein Synthesis at Developing Synapses |
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Requirement for Protein Synthesis at Developing Synapses |
| title_short |
Requirement for Protein Synthesis at Developing Synapses |
| title_sort |
requirement for protein synthesis at developing synapses |
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General Neuroscience |
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http://dx.doi.org/10.1523/jneurosci.2613-09.2009 |
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2009 |
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9778-9793 |
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<jats:p>Activity and protein synthesis act cooperatively to generate persistent changes in synaptic responses. This forms the basis for enduring memory in adults. Activity also shapes neural circuits developmentally, but whether protein synthesis plays a congruent function in this process is poorly understood. Here, we show that brief periods of global or local protein synthesis inhibition decrease the synaptic vesicles available for fusion and increase synapse elimination. Ca<jats:sup>2+</jats:sup>/calmodulin-dependent protein kinase II (CaMKII) is a critical target; its levels are controlled by rapid turnover, and blocking its activity or knocking it down recapitulates the effects of protein synthesis inhibition. Mature presynaptic terminals show decreased sensitivity to protein synthesis inhibition, and resistance coincides with a developmental switch in regulation from CaMKII to PKA (protein kinase A). These findings demonstrate a novel mechanism regulating presynaptic activity and synapse elimination during development, and suggest that protein translation acts coordinately with activity to selectively stabilize appropriate synaptic interactions.</jats:p> |
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| author | Sebeo, Joseph, Hsiao, Kuangfu, Bozdagi, Ozlem, Dumitriu, Dani, Ge, Yongchao, Zhou, Qiang, Benson, Deanna L. |
| author_facet | Sebeo, Joseph, Hsiao, Kuangfu, Bozdagi, Ozlem, Dumitriu, Dani, Ge, Yongchao, Zhou, Qiang, Benson, Deanna L., Sebeo, Joseph, Hsiao, Kuangfu, Bozdagi, Ozlem, Dumitriu, Dani, Ge, Yongchao, Zhou, Qiang, Benson, Deanna L. |
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| description | <jats:p>Activity and protein synthesis act cooperatively to generate persistent changes in synaptic responses. This forms the basis for enduring memory in adults. Activity also shapes neural circuits developmentally, but whether protein synthesis plays a congruent function in this process is poorly understood. Here, we show that brief periods of global or local protein synthesis inhibition decrease the synaptic vesicles available for fusion and increase synapse elimination. Ca<jats:sup>2+</jats:sup>/calmodulin-dependent protein kinase II (CaMKII) is a critical target; its levels are controlled by rapid turnover, and blocking its activity or knocking it down recapitulates the effects of protein synthesis inhibition. Mature presynaptic terminals show decreased sensitivity to protein synthesis inhibition, and resistance coincides with a developmental switch in regulation from CaMKII to PKA (protein kinase A). These findings demonstrate a novel mechanism regulating presynaptic activity and synapse elimination during development, and suggest that protein translation acts coordinately with activity to selectively stabilize appropriate synaptic interactions.</jats:p> |
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| spelling | Sebeo, Joseph Hsiao, Kuangfu Bozdagi, Ozlem Dumitriu, Dani Ge, Yongchao Zhou, Qiang Benson, Deanna L. 0270-6474 1529-2401 Society for Neuroscience General Neuroscience http://dx.doi.org/10.1523/jneurosci.2613-09.2009 <jats:p>Activity and protein synthesis act cooperatively to generate persistent changes in synaptic responses. This forms the basis for enduring memory in adults. Activity also shapes neural circuits developmentally, but whether protein synthesis plays a congruent function in this process is poorly understood. Here, we show that brief periods of global or local protein synthesis inhibition decrease the synaptic vesicles available for fusion and increase synapse elimination. Ca<jats:sup>2+</jats:sup>/calmodulin-dependent protein kinase II (CaMKII) is a critical target; its levels are controlled by rapid turnover, and blocking its activity or knocking it down recapitulates the effects of protein synthesis inhibition. Mature presynaptic terminals show decreased sensitivity to protein synthesis inhibition, and resistance coincides with a developmental switch in regulation from CaMKII to PKA (protein kinase A). These findings demonstrate a novel mechanism regulating presynaptic activity and synapse elimination during development, and suggest that protein translation acts coordinately with activity to selectively stabilize appropriate synaptic interactions.</jats:p> Requirement for Protein Synthesis at Developing Synapses The Journal of Neuroscience |
| spellingShingle | Sebeo, Joseph, Hsiao, Kuangfu, Bozdagi, Ozlem, Dumitriu, Dani, Ge, Yongchao, Zhou, Qiang, Benson, Deanna L., The Journal of Neuroscience, Requirement for Protein Synthesis at Developing Synapses, General Neuroscience |
| title | Requirement for Protein Synthesis at Developing Synapses |
| title_full | Requirement for Protein Synthesis at Developing Synapses |
| title_fullStr | Requirement for Protein Synthesis at Developing Synapses |
| title_full_unstemmed | Requirement for Protein Synthesis at Developing Synapses |
| title_short | Requirement for Protein Synthesis at Developing Synapses |
| title_sort | requirement for protein synthesis at developing synapses |
| title_unstemmed | Requirement for Protein Synthesis at Developing Synapses |
| topic | General Neuroscience |
| url | http://dx.doi.org/10.1523/jneurosci.2613-09.2009 |