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Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction

Tai, Hwan-Ching and Schuman, Erin M. (2008) Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nature Reviews. Neuroscience, 9 (11). pp. 826-838. ISSN 1471-003X.

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Eukaryotic protein degradation by the proteasome and the lysosome is a dynamic and complex process in which ubiquitin has a key regulatory role. The distinctive morphology of the postmitotic neuron creates unique challenges for protein degradation systems with respect to cell-surface protein turnover and substrate delivery to proteolytic machineries that are required for both synaptic plasticity and self-renewal. Moreover, the discovery of ubiquitin-positive protein aggregates in a wide spectrum of neurodegenerative diseases underlines the importance and vulnerability of the degradative system in neurons. In this article, we discuss the molecular mechanism of protein degradation in the neuron with respect to both its function and its dysfunction.

Item Type:Article
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Schuman, Erin M.0000-0002-7053-1005
Additional Information:© 2008 Nature Publishing Group. The authors thank C.-Y. Tai and Y. Yoon for manuscript suggestions and the support of the Howard Hughes Medical Institute.
Funding AgencyGrant Number
Howard Hughes Medical InstituteUNSPECIFIED
Subject Keywords:long-term potentiation; Lewy body disease; Parkinsons-disease; mental-retardation; 26S proteasome; neurodegenerative disease; molecular pathogenesis; dependent proteolysis; interacting proteins; synaptic plasticity
Issue or Number:11
Record Number:CaltechAUTHORS:TAInrn08
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:13411
Deposited By: Tony Diaz
Deposited On:08 May 2009 21:41
Last Modified:09 Mar 2020 13:19

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