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Role of ELAV-like RNA-binding proteins HuD and HuR in the post-transcriptional regulation of acetylcholinesterase in neurons and skeletal muscle cells.
- Source :
-
Chemico-biological interactions [Chem Biol Interact] 2005 Dec 15; Vol. 157-158, pp. 43-9. Date of Electronic Publication: 2005 Oct 20. - Publication Year :
- 2005
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Abstract
- Over the last few years, several laboratories have focused their attention on elucidating the molecular events that control the expression and localization of acetylcholinesterase (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.
- Subjects :
- Acetylcholinesterase genetics
Animals
Cell Differentiation
ELAV Proteins chemistry
Humans
Muscle, Skeletal cytology
Rats
Transcription, Genetic
Acetylcholinesterase metabolism
ELAV Proteins metabolism
Gene Expression Regulation, Enzymologic genetics
Muscle, Skeletal enzymology
Neurons enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0009-2797
- Volume :
- 157-158
- Database :
- MEDLINE
- Journal :
- Chemico-biological interactions
- Publication Type :
- Academic Journal
- Accession number :
- 16242680
- Full Text :
- https://doi.org/10.1016/j.cbi.2005.10.004