Journal of Molecular Neuroscience

, Volume 40, Issue 1, pp 177–184

The Ubiquitin–Proteasome System Regulates the Stability of Neuronal Nicotinic Acetylcholine Receptors


DOI: 10.1007/s12031-009-9272-x

Cite this article as:
Rezvani, K., Teng, Y. & De Biasi, M. J Mol Neurosci (2010) 40: 177. doi:10.1007/s12031-009-9272-x


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.


Nicotinic acetylcholine receptor Protein trafficking Ubiquitin Proteasome Lysosome 

Copyright information

© Humana Press 2009

Authors and Affiliations

  • Khosrow Rezvani
    • 1
  • Yanfen Teng
    • 1
  • Mariella De Biasi
    • 1
    • 2
  1. 1.Department of NeuroscienceBaylor College of MedicineHoustonUSA
  2. 2.Graduate Program in Translational Biology and Molecular MedicineBaylor College of MedicineHoustonUSA

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