title: Ubiquitin proteasome system-mediated degradation of synaptic proteins: An update from the postsynaptic side.
abstract: The ubiquitin proteasome system is one of the principle mechanisms for the regulation of protein homeostasis in mammalian cells. In dynamic cellular structures such as neuronal synapses, ubiquitin proteasome system and protein translation provide an efficient way for cells to respond promptly to local stimulation and regulate neuroplasticity. The majority of research related to long-term plasticity has been focused on the postsynapses and has shown that ubiquitination and subsequent degradation of specific proteins are involved in various activity-dependent plasticity events. This review summarizes recent achievements in understanding ubiquitination of postsynaptic proteins and its impact on synapse plasticity and discusses the direction for advancing future research in the field.
authors.affiliation: Department of Molecular and Integrative Physiology, School of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: nptsai@illinois.edu.
authors.forename: Nien-Pei
authors.initials: NP
authors.lastname: Tsai
keywords: E3 ligase; Neuronal activity; Plasticity; Proteasome; Synapse; Ubiquitination