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J Mol Neurosci. 2010 Jan;40(1-2):177-84. doi: 10.1007/s12031-009-9272-x. Epub 2009 Aug 20.

The ubiquitin-proteasome system regulates the stability of neuronal nicotinic acetylcholine receptors.

Author information

1
Department of Neuroscience, Baylor College of Medicine, Houston, TX 77030, USA.

Abstract

Ubiquitination is a key event for protein degradation by the proteasome system, membrane protein internalization, and protein trafficking among cellular compartments. Few data are available on the role of the ubiquitin-proteasome system (UPS) in the trafficking of neuronal nicotinic acetylcholine receptors (nAChRs). Experiments conducted in neuron-like differentiated rat pheochromocytoma cells (PC12 cells) show that the alpha3, beta2, and beta4 nAChR subunits are ubiquitinated and that their ubiquitination is necessary for degradation. A 24-h treatment with the proteasome inhibitor PS-341 increased the total levels of alpha3 and the two beta subunits in both whole cell lysates and fractions enriched for the ER/Golgi compartment. nAChR subunit upregulation was also detected in plasma membrane-enriched fractions. Inhibition of the lysosomal degradation machinery by E-64 had a significantly smaller effect on nAChR turnover. The present data, together with previous results showing that the alpha7 nAChR subunit is a target of the UPS, point to a prominent role of the proteasome in nAChR trafficking.

PMID:
19693707
PMCID:
PMC3119567
DOI:
10.1007/s12031-009-9272-x
[Indexed for MEDLINE]
Free PMC Article

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