The ubiquitin-specific protease 14 (USP14) is a critical regulator of long-term memory formation
- Timothy J. Jarome1,
- Janine L. Kwapis1,
- Jada J. Hallengren2,
- Scott M. Wilson2 and
- Fred J. Helmstetter1,3
- 1Department of Psychology, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53201, USA
- 2Department of Neurobiology, University of Alabama, Birmingham, Alabama 35294, USA
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.
Footnotes
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↵3 Corresponding author
E-mail fjh{at}uwm.edu
- Received August 7, 2013.
- Accepted October 14, 2013.
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