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Updated: May 4, 2026

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
Published on: May 21, 2019
The ubiquitin-specific protease 14 (USP14) is a critical regulator of long-term memory formation
Timothy J Jarome1, Janine L Kwapis, Jada J Hallengren
1Department of Psychology, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53201, 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.
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