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Cells 2014, 3(2), 258-287; doi:10.3390/cells3020258

Post-Translational Modifications of TRP Channels

*  and
Department of Biosensorics, Institute of Physiology, Universität Hohenheim, 70599 Stuttgart, Germany
* Author to whom correspondence should be addressed.
Received: 28 February 2014 / Revised: 25 March 2014 / Accepted: 27 March 2014 / Published: 8 April 2014
(This article belongs to the Special Issue Transient Receptor Potential (TRP) Channels)
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Transient receptor potential (TRP) channels constitute an ancient family of cation channels that have been found in many eukaryotic organisms from yeast to human. TRP channels exert a multitude of physiological functions ranging from Ca2+ homeostasis in the kidney to pain reception and vision. These channels are activated by a wide range of stimuli and undergo covalent post-translational modifications that affect and modulate their subcellular targeting, their biophysical properties, or channel gating. These modifications include N-linked glycosylation, protein phosphorylation, and covalent attachment of chemicals that reversibly bind to specific cysteine residues. The latter modification represents an unusual activation mechanism of ligand-gated ion channels that is in contrast to the lock-and-key paradigm of receptor activation by its agonists. In this review, we summarize the post-translational modifications identified on TRP channels and, when available, explain their physiological role.
Keywords: post-translational modification; TRP channels; N-linked glycosylation; covalent modification of cysteines; phosphorylation post-translational modification; TRP channels; N-linked glycosylation; covalent modification of cysteines; phosphorylation
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Voolstra, O.; Huber, A. Post-Translational Modifications of TRP Channels. Cells 2014, 3, 258-287.

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