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Protein degradation and protein synthesis in long-term memory formation

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dc.contributor.authorJarome, Timothy J.en
dc.contributor.authorHelmstetter, Fred J.en
dc.contributor.departmentAnimal and Poultry Sciencesen
dc.date.accessioned2018-11-19T18:32:03Zen
dc.date.available2018-11-19T18:32:03Zen
dc.date.issued2014-06-26en
dc.description.abstractLong-term memory (LTM) formation requires transient changes in the activity of intracellular signaling cascades that are thought to regulate new gene transcription and de novo protein synthesis in the brain. Consistent with this, protein synthesis inhibitors impair LTM for a variety of behavioral tasks when infused into the brain around the time of training or following memory retrieval, suggesting that protein synthesis is a critical step in LTM storage in the brain. However, evidence suggests that protein degradation mediated by the ubiquitin-proteasome system (UPS) may also be a critical regulator of LTM formation and stability following retrieval. This requirement for increased protein degradation has been shown in the same brain regions in which protein synthesis is required for LTM storage. Additionally, increases in the phosphorylation of proteins involved in translational control parallel increases in protein polyubiquitination and the increased demand for protein degradation is regulated by intracellular signaling molecules thought to regulate protein synthesis during LTM formation. In some cases inhibiting proteasome activity can rescue memory impairments that result from pharmacological blockade of protein synthesis, suggesting that protein degradation may control the requirement for protein synthesis during the memory storage process. Results such as these suggest that protein degradation and synthesis are both critical for LTM formation and may interact to properly “consolidate” and store memories in the brain. Here, we review the evidence implicating protein synthesis and degradation in LTM storage and highlight the areas of overlap between these two opposing processes. We also discuss evidence suggesting these two processes may interact to properly form and store memories. LTM storage likely requires a coordinated regulation between protein degradation and synthesis at multiple sites in the mammalian brain.en
dc.description.sponsorshipNational Institute of Mental Healthen
dc.description.sponsorshipNIMH: R01-06558en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.3389/fnmol.2014.00061en
dc.identifier.urihttp://hdl.handle.net/10919/85886en
dc.identifier.volume7en
dc.language.isoenen
dc.publisherFrontiersen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectubiquitinen
dc.subjectproteasomeen
dc.subjectfear conditioningen
dc.subjectprotein degradationen
dc.subjectprotein synthesisen
dc.subjectamygdalaen
dc.subjecthippocampusen
dc.titleProtein degradation and protein synthesis in long-term memory formationen
dc.title.serialFrontiers in Molecular Neuroscienceen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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Destination Area: Adaptive Brain and Behavior (ABB)
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