Regulation of TRP channels by N-linked glycosylation

Semin Cell Dev Biol. 2006 Dec;17(6):630-7. doi: 10.1016/j.semcdb.2006.11.007. Epub 2006 Dec 1.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbohydrate Conformation
  • Glycosylation
  • Humans
  • Membrane Potentials / physiology
  • Molecular Sequence Data
  • Oligosaccharides / chemistry*
  • Oligosaccharides / metabolism*
  • TRPC Cation Channels / chemistry*
  • TRPC Cation Channels / metabolism*


  • Oligosaccharides
  • TRPC Cation Channels