Regulation of TRP channels by N-linked glycosylation

David M. Cohen

doi:10.1016/j.semcdb.2006.11.007

Regulation of TRP channels by N-linked glycosylation

David M. Cohen

Nephrology and Hypertension

Research output: Contribution to journal › Review article › peer-review

40 Scopus citations

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)
Pages (from-to)	630-637
Number of pages	8
Journal	Seminars in Cell and Developmental Biology
Volume	17
Issue number	6
DOIs	https://doi.org/10.1016/j.semcdb.2006.11.007
State	Published - Dec 2006

Funding

This work was supported by grants from the National Institutes of Health, the Department of Veterans Affairs, and the American Heart Association. The author thanks R. Sullivan for careful reading of the manuscript and helpful comments.

Funders
Author National Institutes of Health National Institutes of Health National Institutes of Health National Institutes of Health The Bev Hartig Huntington's Disease Foundation National Institutes of Health
U.S. Department of Veterans Affairs
American Heart Association/American Stroke Association

Keywords

Ion channel
Review
Transient receptor potential

ASJC Scopus subject areas

Developmental Biology
Cell Biology

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10.1016/j.semcdb.2006.11.007

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title = "Regulation of TRP channels by N-linked glycosylation",

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.",

keywords = "Ion channel, Review, Transient receptor potential",

author = "Cohen, \{David M.\}",

note = "Funding Information: This work was supported by grants from the National Institutes of Health, the Department of Veterans Affairs, and the American Heart Association. The author thanks R. Sullivan for careful reading of the manuscript and helpful comments.",

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T1 - Regulation of TRP channels by N-linked glycosylation

AU - Cohen, David M.

N1 - Funding Information: This work was supported by grants from the National Institutes of Health, the Department of Veterans Affairs, and the American Heart Association. The author thanks R. Sullivan for careful reading of the manuscript and helpful comments.

PY - 2006/12

Y1 - 2006/12

N2 - 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.

AB - 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.

KW - Ion channel

KW - Review

KW - Transient receptor potential

UR - https://www.scopus.com/pages/publications/33846491396

UR - https://www.scopus.com/pages/publications/33846491396#tab=citedBy

U2 - 10.1016/j.semcdb.2006.11.007

DO - 10.1016/j.semcdb.2006.11.007

M3 - Review article

C2 - 17215147

AN - SCOPUS:33846491396

SN - 1084-9521

VL - 17

SP - 630

EP - 637

JO - Seminars in Cell and Developmental Biology

JF - Seminars in Cell and Developmental Biology

IS - 6

ER -

Regulation of TRP channels by N-linked glycosylation

Abstract

Funding

Keywords

ASJC Scopus subject areas

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