Review
Nature Reviews Neuroscience 3, 854-861 (November 2002) | doi:10.1038/nrn961
Ubiquitin and the synapse
Ashok N. Hegde1 & Aaron DiAntonio2 About the authors
Abstract
Post-translational modification by the attachment of ubiquitin seems to have a crucial role in regulating synaptic structure and function. By controlling the stability, activity and localization of target proteins, this versatile regulatory system can shape the pattern, activity and plasticity of synaptic connections. Here, we discuss the myriad ways in which ubiquitin functions to sculpt synapses during development, and to remodel synapses for the acquisition and storage of memory.
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Author affiliations
- Department of Neurobiology and Anatomy, Wake Forest University Health Sciences, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA.
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Department of Molecular Biology and Pharmacology, Washington University School of Medicine, 660 South Euclid Avenue, St Louis, Missouri 63110, USA.
Email: dianton@molecool.wustl.edu
Correspondence to: Ashok N. Hegde1 Email: ahegde@wfubmc.edu
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