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  Activity-dependent dynamics and sequestration of proteasomes in dendritic spines

Bingol, B., & Schuman, E. M. (2006). Activity-dependent dynamics and sequestration of proteasomes in dendritic spines. Nature, 441(7097), 1144-8. doi:10.1038/nature04769.

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Bingol, B., Author
Schuman, Erin M.1, Author              
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1Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              

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Free keywords: Actins/metabolism Animals Cells, Cultured Cytoskeleton/metabolism Dendritic Spines/drug effects/*metabolism Hippocampus/cytology Photobleaching Potassium Chloride/pharmacology Proteasome Endopeptidase Complex/chemistry/drug effects/*metabolism Protein Binding Rats Receptors, N-Methyl-D-Aspartate/metabolism Synapses/chemistry/drug effects/metabolism
 Abstract: The regulated degradation of proteins by the ubiquitin proteasome pathway is emerging as an important modulator of synaptic function and plasticity. The proteasome is a large, multi-subunit cellular machine that recognizes, unfolds and degrades target polyubiquitinated proteins. Here we report NMDA (N-methyl-D-aspartate) receptor-dependent redistribution of proteasomes from dendritic shafts to synaptic spines upon synaptic stimulation, providing a mechanism for local protein degradation. Using a proteasome-activity reporter and local perfusion, we show that synaptic stimulation regulates proteasome activity locally in the dendrites. We used restricted photobleaching of individual spines and dendritic shafts to reveal the dynamics that underlie proteasome sequestration, and show that activity modestly enhances the entry rate of proteasomes into spines while dramatically reducing their exit rate. Proteasome sequestration is persistent, reflecting an association with the actin-based cytoskeleton. Together, our data indicate that synaptic activity can promote the recruitment and sequestration of proteasomes to locally remodel the protein composition of synapses.

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 Dates: 2006-07-01
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: Other: 16810255
DOI: 10.1038/nature04769
ISSN: 1476-4687 (Electronic)0028-0836 (Linking)
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Title: Nature
Source Genre: Journal
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Pages: - Volume / Issue: 441 (7097) Sequence Number: - Start / End Page: 1144 - 8 Identifier: -