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Physiology 20: 398-407, 2005; doi:10.1152/physiol.00033.2005
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Physiology, Vol. 20, No. 6, 398-407, December 2005
© 2005 Int. Union Physiol. Sci./Am. Physiol. Soc.

REVIEW

Ubiquitylation of Ion Channels

Hugues Abriel1,2 and Olivier Staub1

1 Department of Pharmacology and Toxicology and
2 Service of Cardiology, University of Lausanne, Switzerland

Hugues.Abriel{at}unil.ch Olivier.Staub{at}unil.ch

Ubiquitylation (i.e., covalent attachment of ubiquitin moieties to proteins) of ion channels allows regulation of their activity and fate. Nedd4/Nedd4-like ubiquitin-protein ligases bind to, ubiquitylate, and modulate the internalization of several channels bearing PY motifs, whereas endoplasmic reticulum-associated degradation (involving ubiquitylation) plays an important role in the biogenesis of normal and defective channels.




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