title: Ubiquitin and protein turnover in synapse function.
abstract: Enduring modification of synapses is central to long-lasting neural circuit plasticity. Such adaptations include rapid posttranslational modification of existing synaptic proteins over periods of minutes and persisting changes in the abundance of synaptic proteins over hours to days. Recently, ubiquitination and protein degradation have emerged as additional mechanisms for modifying the function and molecular composition of synapses. These recent findings raise intriguing questions as to how enduring changes at synapses are accomplished in the face of robust, ongoing molecular turnover.
authors.affiliation: Department of Neurobiology, Duke University Medical Center, Box 3209, Durham, North Carolina 27710, USA.
authors.forename: Jason J
authors.initials: JJ
authors.lastname: Yi
authors.forename: Michael D
authors.initials: MD
authors.lastname: Ehlers
mesh_terms: D000818:Animals; D006801:Humans; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009473:Neuronal Plasticity; D018377:Neurotransmitter Agents / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000502:physiology; D013116:Spinal Cord / Q000502:physiology; D013569:Synapses / Q000378:metabolism* / Q000502:physiology*; D025801:Ubiquitin / Q000502:physiology*
chemical_list: D009419:Nerve Tissue Proteins; D018377:Neurotransmitter Agents; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex