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

Khosrow Rezvani, Yanfen Teng, Mariella De Biasi

Research output: Contribution to journalArticle

35 Scopus citations

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 α3, β2, and β4 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 α3 and the two β 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 α7 nAChR subunit is a target of the UPS, point to a prominent role of the proteasome in nAChR trafficking.

Original languageEnglish (US)
Pages (from-to)177-184
Number of pages8
JournalJournal of Molecular Neuroscience
Volume40
Issue number1-2
DOIs
StatePublished - Jan 2010

Keywords

  • Lysosome
  • Nicotinic acetylcholine receptor
  • Proteasome
  • Protein trafficking
  • Ubiquitin

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience

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