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  Synaptic protein degradation by the ubiquitin proteasome system

Bingol, B., & Schuman, E. M. (2005). Synaptic protein degradation by the ubiquitin proteasome system. Curr Opin Neurobiol, 15(5), 536-41. doi:10.1016/j.conb.2005.08.016.

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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: Animals Humans Neuronal Plasticity/*physiology Proteasome Endopeptidase Complex/*metabolism Proteins/*metabolism Synapses/*metabolism Ubiquitin/*metabolism
 Abstract: Synaptic plasticity -- the modulation of synaptic strength between a presynaptic terminal and a postsynaptic dendrite -- is thought to be a mechanism that underlies learning and memory. It has become increasingly clear that regulated protein synthesis is an important mechanism used to regulate the protein content of synapses that results in changes in synaptic strength. Recent experiments have highlighted a role for the opposing process, that is, regulated protein degradation via the ubiquitin-proteasome system, in synaptic plasticity. These recent findings raise exciting questions as to how proteasomal activity can regulate synapses over different temporal and spatial scales.

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 Dates: 2005-09-10
 Publication Status: Issued
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 Identifiers: Other: 16150592
DOI: 10.1016/j.conb.2005.08.016
ISSN: 0959-4388 (Print)0959-4388 (Linking)
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Title: Curr Opin Neurobiol
Source Genre: Journal
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Pages: - Volume / Issue: 15 (5) Sequence Number: - Start / End Page: 536 - 41 Identifier: -