Egan TJ Acuña MA Zenobi-Wong M Zeilhofer HU Urech D 2016 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. application/pdf https://sonar.ch/global/documents/220634 eng info:eu-repo/semantics/altIdentifier/doi/10.1042/BSR20160149 info:eu-repo/semantics/altIdentifier/pmid/27582506 info:eu-repo/semantics/openAccess Bioscience reports. - 2016 glycoproteins glycosylation ion channels transient receptor potential channels Effects of N-Glycosylation of the human cation channel TRPA1 on agonist-sensitivity. http://purl.org/coar/resource_type/c_6501