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PMID: 19079132 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Think locally: control of ubiquitin-dependent protein degradation in neurons.

EMBO reports ·Vol. 10 ·No. 1 ·2009-01-00 ·Pages 44-50

Segref A, Hoppe T

Abstract

The nervous system coordinates many aspects of body function such as learning, memory, behaviour and locomotion. Therefore, it must develop and maintain an intricate network of differentiated neuronal cells, which communicate efficiently with each other and with non-neuronal target cells. Unlike most somatic cells, differentiated neurons are post-mitotic and characterized by a highly polarized morphology that determines the flow of information. Among other post-translational modifications, the ubiquitination of specific protein substrates was recently shown to have a crucial role in the regulation of neuronal development and differentiation. Here, we review recent findings that illustrate the mechanisms that mediate the temporal and spatial control of neuronal protein turnover by the ubiquitin-proteasome system (UPS), which is crucial for the development and function of the nervous system.

MeSH Terms
Animals Humans Neurons/metabolism Proteasome Endopeptidase Complex/metabolism Protein Processing, Post-Translational Synapses/metabolism Ubiquitin/metabolism
Chemicals
Ubiquitin Proteasome Endopeptidase Complex
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Segref Alexandra
Centre for Molecular Neurobiology, ZMNH, University of Hamburg, Hamburg, Germany.
Hoppe Thorsten
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Article Info
Journal
EMBO reports
Abbr.
EMBO Rep
ISSN
1469-3178
Published
2009-01-00
Epub
2008-00-12
Pages
44-50
Language
English
Region
England
NLM ID
100963049
PMCID
PMC2613211
Subset
IM
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