VAMP7 regulates constitutive membrane incorporation of the cold-activated channel TRPM8

Debapriya Ghosh, Silvia Pinto, Lydia Danglot, Ine Vandewauw, Andrei Segal, Nele Van Ranst, Melissa Benoit, Annelies Janssens, Rudi Vennekens, Pieter Vanden Berghe, Thierry Galli, Joris Vriens and Thomas Voets ()
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Debapriya Ghosh: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Silvia Pinto: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Lydia Danglot: Institut Jacques Monod, CNRS UMR 7592, University of Paris Diderot
Ine Vandewauw: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Andrei Segal: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Nele Van Ranst: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Melissa Benoit: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Annelies Janssens: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Rudi Vennekens: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Pieter Vanden Berghe: Laboratory for Enteric NeuroScience, University of Leuven
Thierry Galli: Institut Jacques Monod, CNRS UMR 7592, University of Paris Diderot
Joris Vriens: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven
Thomas Voets: Laboratory of Ion Channel Research and TRP Channel Research Platform Leuven (TRPLe), University of Leuven

Nature Communications, 2016, vol. 7, issue 1, 1-15

Abstract: Abstract The cation channel TRPM8 plays a central role in the somatosensory system, as a key sensor of innocuously cold temperatures and cooling agents. Although increased functional expression of TRPM8 has been implicated in various forms of pathological cold hypersensitivity, little is known about the cellular and molecular mechanisms that determine TRPM8 abundance at the plasma membrane. Here we demonstrate constitutive transport of TRPM8 towards the plasma membrane in atypical, non-acidic transport vesicles that contain lysosomal-associated membrane protein 1 (LAMP1), and provide evidence that vesicle-associated membrane protein 7 (VAMP7) mediates fusion of these vesicles with the plasma membrane. In line herewith, VAMP7-deficient mice exhibit reduced functional expression of TRPM8 in sensory neurons and concomitant deficits in cold avoidance and icilin-induced cold hypersensitivity. Our results uncover a cellular pathway that controls functional plasma membrane incorporation of a temperature-sensitive TRP channel, and thus regulates thermosensitivity in vivo.

Date: 2016
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DOI: 10.1038/ncomms10489

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