Regulation of TRP channels by N-linked glycosylation

Research output: Contribution to journalReview articlepeer-review

40 Scopus citations


A subset of TRP channel proteins undergoes regulatory N-linked glycosylation. A glycosylation site in the first extracellular loop of TRPV5 is enzymatically cleaved by a secreted glucuronidase, indirectly regulating channel function. Members of the TRPC family share a similar site, although details about a regulatory role are lacking. A second conserved TRP channel glycosylation site is found immediately adjacent to the channel pore-forming loop; both TRPV1 and TRPV4 - and perhaps other TRPV family members - are influenced by glycosylation at this site. N-linked glycosylation, and the dynamic regulation of this process, substantially impacts function and targeting of TRP channels.

Original languageEnglish (US)
Pages (from-to)630-637
Number of pages8
JournalSeminars in Cell and Developmental Biology
Issue number6
StatePublished - Dec 2006


  • Ion channel
  • Review
  • Transient receptor potential

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology


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