Journal
CELLS
Volume 3, Issue 2, Pages 258-287Publisher
MDPI
DOI: 10.3390/cells3020258
Keywords
post-translational modification; TRP channels; N-linked glycosylation; covalent modification of cysteines; phosphorylation
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Funding
- Deutsche Forschungsgemeinschaft [VO1741/1-1, HU839/2-6]
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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.
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