Role of ELAV-like RNA-binding proteins HuD and HuR in the post-transcriptional regulation of acetylcholinesterase in neurons and skeletal muscle cells

被引:16
|
作者
Deschênes-Furry, J
Angus, LM
Bélanger, G
Mwanjewe, J
Jasmin, BJ [1 ]
机构
[1] Univ Ottawa, Fac Med, Dept Cellular & Mol Med, Ottawa, ON K1H 8M5, Canada
[2] Univ Ottawa, Fac Med, Ctr Neuromuscular Dis, Ottawa, ON K1H 8M5, Canada
关键词
neuromuscular junction; synaptic proteins; differentiation; mRNA stability; AU-rich element;
D O I
10.1016/j.cbi.2005.10.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Over the last few years, several laboratories have focused their attention on elucidating the molecular events that control the expression and localization of acetyleholinesterase (AChE) in neurons and skeletal muscle cells. In this context, results from a number of studies have clearly shown the important contribution of transcriptional events in regulating AChE expression. Specifically, these studies have highlighted the roles of several cis- and trans-acting factors that control transcription of the AChE gene in these excitable cells. However, it has also become apparent that changes in the transcriptional activity of the AChE gene cannot fully account for the alterations seen in the overall abundance of AChE transcripts in neurons and muscle cells placed under a variety of experimental conditions. This indicates, therefore, that post-transcriptional mechanisms also play a significant role in controlling AChE mRNA expression. With this in mind, we have recently begun to address this issue in greater detail. Here, we provide a summary of our most recent findings dealing with the post-transcriptional regulation of AChE. Together, our studies have shown so far the important contribution of an AU-rich element located in the 3'UTR of AChE transcripts and of the stabilizing RNA-binding proteins of the ELAV-like family in regulating AChE expression in differentiating neuronal and muscle cells. (c) 2005 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:43 / 49
页数:7
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