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Effects of N-Glycosylation of the human cation channel TRPA1 on agonist-sensitivity.

  • Egan TJ ETH Zürich, Zurich, Switzerland t.egan@numab.com.
  • Acuña MA Institute of Pharmacology & Toxicology, University of Zurich, Zurich, Switzerland.
  • Zenobi-Wong M Cartilage Engineering & Regeneration Lab, the Department of Health, Science & Technology, ETH Zürich, Zurich, Switzerland.
  • Zeilhofer HU Institute of Pharmacology & Toxicology, University of Zurich, Zurich, Switzerland.
  • Urech D Numab AG, Wädenswil, Switzerland.
  • 2016-09-02
Published in:
  • Bioscience reports. - 2016
glycoproteins
glycosylation
ion channels
transient receptor potential channels
English Determining the functional significance of post-translational modifications advances our understanding of many broadly-expressed proteins, and particularly ion channels. The enzymes that catalyze these modifications are often expressed in a cell-type specific manner, resulting in considerable structural diversity among post-translationally modified proteins that are expressed across a variety of cell types. TRP channels exhibit notably variable behavior between cell types in vitro and in vivo , and they are frequently modified with N-glycans that contribute to protein function. TRPA1 possesses two putative N-linked glycosylation sites at N747 and N753 that have not yet been studied in detail. Here, we show that both of these sites can be modified with an N-glycan and that the glycan at position N747 modulates agonist-sensitivity of TRPA1 in vitro Additionally, we found that N-glycosylation also modulates cooperative effects of temperature and the agonist cinnamaldehyde on TRPA1 channel activation. Collectively, these findings suggest a dynamic role played by the N-glycosylation of human TRPA1. They also provide further evidence of the versatility of N-glycans and will assist in efforts to fully understand the complex regulation of TRPA1 activity.
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  • English
Open access status
gold
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https://sonar.ch/global/documents/220634
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