Header

UZH-Logo

Maintenance Infos

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


Egan, Timothy James; Acuña, Mario A; Zenobi-Wong, Marcy; Zeilhofer, Hanns Ulrich; Urech, David (2016). Effects of N-Glycosylation of the human cation channel TRPA1 on agonist-sensitivity. Bioscience Reports, 36(5):e00390-e00390.

Abstract

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.

Abstract

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.

Statistics

Citations

3 citations in Web of Science®
3 citations in Scopus®
Google Scholar™

Altmetrics

Downloads

7 downloads since deposited on 07 Sep 2016
6 downloads since 12 months
Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Pharmacology and Toxicology
07 Faculty of Science > Institute of Pharmacology and Toxicology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:31 August 2016
Deposited On:07 Sep 2016 12:40
Last Modified:08 Dec 2017 20:20
Publisher:Portland Press
ISSN:0144-8463
Free access at:PubMed ID. An embargo period may apply.
Publisher DOI:https://doi.org/10.1042/BSR20160149
PubMed ID:27582506

Download

Download PDF  'Effects of N-Glycosylation of the human cation channel TRPA1 on agonist-sensitivity'.
Preview
Content: Accepted Version
Filetype: PDF
Size: 790kB
View at publisher