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The Xenopus TRPV6 homolog encodes a Mg 2+ ‐permeant channel that is inhibited by interaction with TRPC1
Author(s) -
Courjaret Raphael,
Hubrack Satanay,
Daalis Arwa,
Dib Maya,
Machaca Khaled
Publication year - 2013
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.24411
Subject(s) - xenopus , microbiology and biotechnology , chemistry , endogeny , trpv6 , oocyte , biophysics , transient receptor potential channel , hek 293 cells , trpc1 , biology , gene , biochemistry , receptor , embryo
The TRP gene family encodes primarily cation non‐selective, Ca 2+ permeant channels that are involved in a dizzying array of sensory mechanisms. Two channels in this large family TRPV5 and TRPV6 are highly Ca 2+ selective and are expressed in epithelia where they are important in Ca 2+ uptake. TRPV5/6 are constitutively active, yet the mechanisms regulating their activation in native tissue remains elusive. Here we functionally characterize the Xenopus TRPV6 homolog. xTRPV6 is expressed in the oocyte and encodes a channel that is permeant to divalents including Ca 2+ , and displays a high permeability to Mg 2+ . The oocyte does not exhibit functional TRPV6‐like current at rest, showing that the endogenous channel is somehow maintained in an inactive state. We show that endogenous as well as overexpressed xTRPV6 interacts with xTRPC1 and that this interaction inhibits xTRPV6 currents. As such TRPC1 is likely to regulate the activity of TRPV6 under physiological conditions. J. Cell. Physiol. 228: 2386–2398, 2013. © 2013 The Authors. Journal of Cellular Physiology Published by Wiley Periodicals, Inc.