Abstract
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 language | English (US) |
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Pages (from-to) | 630-637 |
Number of pages | 8 |
Journal | Seminars in Cell and Developmental Biology |
Volume | 17 |
Issue number | 6 |
DOIs | |
State | Published - Dec 2006 |
Keywords
- Ion channel
- Review
- Transient receptor potential
ASJC Scopus subject areas
- Developmental Biology
- Cell Biology