The ubiquitin-specific protease 14 (USP14) is a critical regulator of long-term memory formation

被引:35
|
作者
Jarome, Timothy J. [1 ]
Kwapis, Janine L. [1 ]
Hallengren, Jada J. [2 ]
Wilson, Scott M. [2 ]
Helmstetter, Fred J. [1 ]
机构
[1] Univ Wisconsin, Dept Psychol, Milwaukee, WI 53201 USA
[2] Univ Alabama Birmingham, Dept Neurobiol, Birmingham, AL 35294 USA
基金
美国国家卫生研究院;
关键词
SYNAPTIC PLASTICITY; FEAR MEMORY; ATAXIA MICE; KINASE-A; DEGRADATION; EXPRESSION; CONSOLIDATION; MAINTENANCE; SYSTEM; PHOSPHORYLATION;
D O I
10.1101/lm.032771.113
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
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.
引用
收藏
页码:9 / 13
页数:5
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