Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 304K) PPT slides of all figures Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Korhonen, L. Articles by Lindholm, D. Search for Related Content PubMed PubMed Citation Articles by Korhonen, L. Articles by Lindholm, D. Social Bookmarking                            What's this?

The ubiquitin proteasome system in synaptic and axonal degeneration

Laura Korhonen^1,2 and Dan Lindholm^1,2

¹ Department of Neuroscience, Unit of Neurobiology, Biomedical Centre, Uppsala University, S-75123 Uppsala, Sweden
² Mclean Hospital, Harvard Medical School, Belmont, MA 02478

Address correspondence to Dan Lindholm, Dept. of Neuroscience, Unit of Neurobiology, Biomedical Centre, Box 587, Uppsala University, S-75123 Uppsala, Sweden. Tel.: 46-18-471-4435. Fax: 46-18-559-017. email: dan.lindholm{at}neuro.uu.se

The ubiquitin proteasome system (UPS) contributes to the pathophysiology of neurodegenerative diseases, and it is also a major determinant of synaptic protein degradation and activity. Recent studies in rodents and in the fruit fly Drosophila have shown that the activity of the UPS is involved in axonal degeneration. Increased knowledge of the UPS in synaptic and axonal reactions may provide novel drug targets for treatments of neuronal injuries and neurodegenerative disorders.

Key Words: neurodegeneration; synapse function; Wallerian degeneration; polyubiquitination; monoubiquitination

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Wang, J., Wang, C.-E., Orr, A., Tydlacka, S., Li, S.-H., Li, X.-J. (2008). Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. JCB 180: 1177-1189 [Abstract] [Full Text]  
• Wishart, T. M., Paterson, J. M., Short, D. M., Meredith, S., Robertson, K. A., Sutherland, C., Cousin, M. A., Dutia, M. B., Gillingwater, T. H. (2007). Differential Proteomics Analysis of Synaptic Proteins Identifies Potential Cellular Targets and Protein Mediators of Synaptic Neuroprotection Conferred by the Slow Wallerian Degeneration (Wlds) Gene. Mol. Cell. Proteomics 6: 1318-1330 [Abstract] [Full Text]  
• Dickey, C. A., Yue, M., Lin, W.-L., Dickson, D. W., Dunmore, J. H., Lee, W. C., Zehr, C., West, G., Cao, S., Clark, A. M. K., Caldwell, G. A., Caldwell, K. A., Eckman, C., Patterson, C., Hutton, M., Petrucelli, L. (2006). Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species.. J. Neurosci. 26: 6985-6996 [Abstract] [Full Text]  
• Gillingwater, T. H., Wishart, T. M., Chen, P. E., Haley, J. E., Robertson, K., MacDonald, S. H.-F., Middleton, S., Wawrowski, K., Shipston, M. J., Melmed, S., Wyllie, D. J.A., Skehel, P. A., Coleman, M. P., Ribchester, R. R. (2006). The neuroprotective WldS gene regulates expression of PTTG1 and erythroid differentiation regulator 1-like gene in mice and human cells. Hum Mol Genet 15: 625-635 [Abstract] [Full Text]  
• Chapman, H., Ramstrom, C., Korhonen, L., Laine, M., Wann, K. T., Lindholm, D., Pasternack, M., Tornquist, K. (2005). Downregulation of the HERG (KCNH2) K+ channel by ceramide: evidence for ubiquitin-mediated lysosomal degradation. J. Cell Sci. 118: 5325-5334 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents