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The ubiquitin-specific protease 14 (USP14) is a critical regulator of long-term memory formation. Learn Mem 2013 Dec 16;21(1):9-13

Date

12/18/2013

Pubmed ID

24344179

Pubmed Central ID

PMC3867711

DOI

10.1101/lm.032771.113

Scopus ID

2-s2.0-84892611707 (requires institutional sign-in at Scopus site)   36 Citations

Abstract

Numerous studies have suggested a role for ubiquitin-proteasome-mediated protein degradation in learning-dependent synaptic plasticity; however, very little is known about how protein degradation is regulated at the level of the proteasome during memory formation. The ubiquitin-specific protease 14 (USP14) is a proteasomal deubiquitinating enzyme that is thought to regulate protein degradation in neurons; however, it is unknown if USP14 is involved in learning-dependent synaptic plasticity. We found that infusion of a USP14 inhibitor into the amygdala impaired long-term memory for a fear conditioning task, suggesting that USP14 is a critical regulator of long-term memory formation in the amygdala.

Author List

Jarome TJ, Kwapis JL, Hallengren JJ, Wilson SM, Helmstetter FJ

Author

Fred Helmstetter PhD Professor in the Psychology / Neuroscience department at University of Wisconsin - Milwaukee




MESH terms used to index this publication - Major topics in bold

Acoustic Stimulation
Amygdala
Analysis of Variance
Animals
Conditioning, Classical
Dose-Response Relationship, Drug
Enzyme Inhibitors
Fear
Male
Memory Disorders
Memory, Long-Term
Rats
Rats, Long-Evans
Ubiquitin Thiolesterase