Regulation of TRP channels by N-linked glycosylation.
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.
Cohen
David M
DM
Division of Nephrology and Hypertension, Department of Medicine, Oregon Health & Science University, Portland Veterans Affairs Medical Center, Portland, OR 97239, USA. cohend@ohsu.edu
D000595:Amino Acid Sequence; D000818:Animals; D002236:Carbohydrate Conformation; D006031:Glycosylation; D006801:Humans; D008564:Membrane Potentials / Q000502:physiology; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry* / Q000378:metabolism*; D050052:TRPC Cation Channels / Q000737:chemistry* / Q000378:metabolism*
D009844:Oligosaccharides; D050052:TRPC Cation Channels