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Neural Plasticity
Volume 2013 (2013), Article ID 432057, 10 pages
Review Article

Ubiquitination of Neurotransmitter Receptors and Postsynaptic Scaffolding Proteins

Department of Biology, Boston University, 5 Cummington Mall, Boston, MA 02215, USA

Received 28 September 2012; Accepted 26 December 2012

Academic Editor: Michael Stewart

Copyright © 2013 Amy W. Lin and Heng-Ye Man. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The human brain is made up of an extensive network of neurons that communicate by forming specialized connections called synapses. The amount, location, and dynamic turnover of synaptic proteins, including neurotransmitter receptors and synaptic scaffolding molecules, are under complex regulation and play a crucial role in synaptic connectivity and plasticity, as well as in higher brain functions. An increasing number of studies have established ubiquitination and proteasome-mediated degradation as universal mechanisms in the control of synaptic protein homeostasis. In this paper, we focus on the role of the ubiquitin-proteasome system (UPS) in the turnover of major neurotransmitter receptors, including glutamatergic and nonglutamatergic receptors, as well as postsynaptic receptor-interacting proteins.