DOI: 10.1146/annurev.neuro.27.070203.144317. UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE

UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE

10.1146/annurev.neuro.27.070203.144317

Crossref journal-article

Annual Reviews

Annual Review of Neuroscience (22)

Abstract

▪ Abstract Posttranslational modification of cellular proteins by the covalent attachment of ubiquitin regulates protein stability, activity, and localization. Ubiquitination is rapid and reversible and is a potent mechanism for the spatial and temporal control of protein activity. By sculpting the molecular composition of the synapse, this versatile posttranslational modification shapes the pattern, activity, and plasticity of synaptic connections. Synaptic processes regulated by ubiquitination, as well as ubiquitination enzymes and their targets at the synapse, are being identified by genetic, biochemical, and electrophysiological analyses. This work provides tantalizing hints that neuronal activity collaborates with ubiquitination pathways to regulate the structure and function of synapses.

Bibliography

DiAntonio, A., & Hicke, L. (2004). UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE. Annual Review of Neuroscience, 27(1), 223â246.

Authors 2

Aaron DiAntonio (first)
Linda Hicke (additional)

References 99 Referenced 151

Dates

Type	When
Created	21 years, 2 months ago (June 24, 2004, 3:32 p.m.)
Deposited	3 years, 10 months ago (Oct. 14, 2021, 3:08 p.m.)
Indexed	1 year, 1 month ago (Aug. 3, 2024, 2:53 p.m.)
Issued	21 years, 1 month ago (July 21, 2004)
Published	21 years, 1 month ago (July 21, 2004)
Published Print	21 years, 1 month ago (July 21, 2004)

Funders 0

None

BibTeX

@article{DiAntonio_2004, title={UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE}, volume={27}, ISSN={1545-4126}, url={http://dx.doi.org/10.1146/annurev.neuro.27.070203.144317}, DOI={10.1146/annurev.neuro.27.070203.144317}, number={1}, journal={Annual Review of Neuroscience}, publisher={Annual Reviews}, author={DiAntonio, Aaron and Hicke, Linda}, year={2004}, month=jul, pages={223–246} }

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  "abstract": "<jats:p> \u25aa Abstract\u2002 Posttranslational modification of cellular proteins by the covalent attachment of ubiquitin regulates protein stability, activity, and localization. Ubiquitination is rapid and reversible and is a potent mechanism for the spatial and temporal control of protein activity. By sculpting the molecular composition of the synapse, this versatile posttranslational modification shapes the pattern, activity, and plasticity of synaptic connections. Synaptic processes regulated by ubiquitination, as well as ubiquitination enzymes and their targets at the synapse, are being identified by genetic, biochemical, and electrophysiological analyses. This work provides tantalizing hints that neuronal activity collaborates with ubiquitination pathways to regulate the structure and function of synapses. </jats:p>",
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