Journal article
N-glycosylation determines ionic permeability and desensitization of the TRPV1 capsaicin receptor
NA Veldhuis, MJ Lew, FC Abogadie, DP Poole, EA Jennings, JJ Ivanusic, H Eilers, NW Bunnett, P McIntyre
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2012
Abstract
The balance of glycosylation and deglycosylation of ion channels can markedly influence their function and regulation. However, the functional importance of glycosylation of the TRPV1 receptor, a key sensor of pain-sensing nerves, is not well understood, and whether TRPV1 is glycosylated in neurons is unclear. We report that TRPV1 is N-glycosylated and that N-glycosylation is a major determinant of capsaicin-evoked desensitization and ionic permeability. Both N-glycosylated and unglycosylated TRPV1 was detected in extracts of peripheral sensory nerves by Western blotting. TRPV1 expressed in HEK-293 cells exhibited various degrees of glycosylation. A mutant of asparagine 604 (N604T) was not g..
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Awarded by National Institute of Diabetes and Digestive and Kidney Diseases
Funding Acknowledgements
This work was supported in whole or in part, by NHMRC Grant 566834 (to P. M. and N. W. B.), 633033 (to N. W. B.) and National Institutes of Health Grants DK57840, DK43207, DK39957 (to N. W. B.).