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

来源：

LEARNING & MEMORY | 2014年 / 21卷 / 01期

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

页码：9 / 13

页数：5

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