ArticleThe Journal of biological chemistry2011
Translational regulation of acetylcholinesterase by the RNA-binding protein Pumilio-2 at the neuromuscular synapse.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Smoking exposure alters splicing of the nicotinic acetylcholine receptor subunit CHRNA5.Human genomics · 2026Article
- Cell type mapping of inflammatory muscle diseases highlights selective myofiber vulnerability in inclusion body myositis.Nature aging · 2024Article
- Dosage sensitivity to Pumilio1 variants in the mouse brain reflects distinct molecular mechanisms.The EMBO journal · 2023Article
- Regulation of Parkinson's disease-associated genes by Pumilio proteins and microRNAs in SH-SY5Y neuronal cells.PloS one · 2022Article
- Cataloguing and Selection of mRNAs Localized to Dendrites in Neurons and Regulated by RNA-Binding Proteins in RNA Granules.Biomolecules · 2020Review
- Pum2 Shapes the Transcriptome in Developing Axons through Retention of Target mRNAs in the Cell Body.Neuron · 2019Article
- Biogenesis, assembly and trafficking of acetylcholinesterase.Journal of neurochemistry · 2017Review
- Synaptic control of local translation: the plot thickens with new characters.Cellular and molecular life sciences : CMLS · 2014Review
- HSCARG inhibits NADPH oxidase activity through regulation of the expression of p47phox.PloS one · 2013Article
- Trans-acting factors governing acetylcholinesterase mRNA metabolism in neurons.Frontiers in molecular neuroscience · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Acetylcholinesterase (AChE) is highly expressed at sites of nerve-muscle contact where it is regulated at both the transcriptional and post-transcriptional levels. Our understanding of the molecular mechanisms underlying its regulation is incomplete, but they appear to involve both translational and post-translational events as well. Here, we show that Pumilio-2 (PUM2), an RNA binding translational repressor, is highly localized at the neuromuscular junction where AChE mRNA concentrates. Immunoprecipitation of muscle cell extracts with a PUM2 specific antibody precipitated AChE mRNA, suggesting that PUM2 binds to the AChE transcripts in a complex. Gel shift assays using a bacterially expressed PUM2 RNA binding domain showed specific binding using wild type AChE 3'-UTR RNA segment that was abrogated by mutation of the consensus recognition site. Transfecting skeletal muscle cells with shRNAs specific for PUM2 up-regulated AChE expression, whereas overexpression of PUM2 decreased AChE activity. We conclude that PUM2 binds to AChE mRNA and regulates AChE expression translationally at the neuromuscular synapse. Finally, we found that PUM2 is regulated by the motor nerve suggesting a trans-synaptic mechanism for locally regulating translation of specific proteins involved in modulating synaptic transmission, analogous to CNS synapses.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.