Next Article in Journal / Special Issue
The Role of Canonical Transient Receptor Potential Channels in Seizure and Excitotoxicity
Previous Article in Journal / Special Issue
PKC-dependent Phosphorylation of the H1 Histamine Receptor Modulates TRPC6 Activity
Cells 2014, 3(2), 258-287; doi:10.3390/cells3020258
Review

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)
View Full-Text   |   Download PDF [1325 KB, 9 April 2014; original version 8 April 2014]   |  

Abstract

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 3.0).
SciFeed

Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
EndNote |
RIS
MDPI and ACS Style

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

View more citation formats

Related Articles

Article Metrics

Comments

[Return to top]
Cells EISSN 2073-4409 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert