Activity dependent protein degradation is critical for the formation and stability of fear memory in the amygdala. PLoS One 2011;6(9):e24349
Date
10/01/2011Pubmed ID
21961035Pubmed Central ID
PMC3178530DOI
10.1371/journal.pone.0024349Scopus ID
2-s2.0-80053089627 (requires institutional sign-in at Scopus site) 153 CitationsAbstract
Protein degradation through the ubiquitin-proteasome system [UPS] plays a critical role in some forms of synaptic plasticity. However, its role in memory formation in the amygdala, a site critical for the formation of fear memories, currently remains unknown. Here we provide the first evidence that protein degradation through the UPS is critically engaged at amygdala synapses during memory formation and retrieval. Fear conditioning results in NMDA-dependent increases in degradation-specific polyubiquitination in the amygdala, targeting proteins involved in translational control and synaptic structure and blocking the degradation of these proteins significantly impairs long-term memory. Furthermore, retrieval of fear memory results in a second wave of NMDA-dependent polyubiquitination that targets proteins involved in translational silencing and synaptic structure and is critical for memory updating following recall. These results indicate that UPS-mediated protein degradation is a major regulator of synaptic plasticity necessary for the formation and stability of long-term memories at amygdala synapses.
Author List
Jarome TJ, Werner CT, Kwapis JL, Helmstetter FJAuthor
Fred Helmstetter PhD Professor in the Psychology / Neuroscience department at University of Wisconsin - MilwaukeeMESH terms used to index this publication - Major topics in bold
AmygdalaAnimals
Cysteine Proteinase Inhibitors
DNA Helicases
Excitatory Amino Acid Antagonists
Fear
Immunoblotting
Lactones
Male
Memory
Memory, Long-Term
N-Methylaspartate
Neuronal Plasticity
Piperidines
Proteasome Endopeptidase Complex
Proteolysis
Rats
Rats, Long-Evans
Receptors, N-Methyl-D-Aspartate
Synapses
Time Factors
Ubiquitin
Ubiquitination
