The Transient Receptor Potential Channel on the Yeast Vacuole Is Mechanosensitive

Ca2+ is released from the vacuole into the yeast cytoplasm on an osmotic upshock, but how this upshock is perceived was unknown. We found the vacuolar channel, Yvc1p, to be mechanosensitive, showing that the Ca2+ conduit is also the sensing molecule. Although fragile, the yeast vacuole allows limite...

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Published in:Proceedings of the National Academy of Sciences - PNAS 2003-06, Vol.100 (12), p.7105-7110
Main Authors: Zhou, Xin-Liang, Batiza, Ann F., Loukin, Stephen H., Palmer, Chris P., Kung, Ching, Saimi, Yoshiro
Format: Article
Language:English
Subjects:
Base Sequence
Biological Sciences
Calcium
Calcium Channels - genetics
Calcium Channels - metabolism
Calcium Signaling
Cell membranes
Cellular biology
Cytoplasm
DNA, Fungal - genetics
Electric potential
Genes, Fungal
Hydrostatic Pressure
Lipid bilayers
Mechanotransduction, Cellular
Membrane Potentials
Models, Biological
Molecules
Osmosis
Osmotic Pressure
P branes
Pressure pulses
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Sensors
TRPC Cation Channels
Vacuoles
Vacuoles - metabolism
Yeast
Yeasts
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Summary:Ca2+ is released from the vacuole into the yeast cytoplasm on an osmotic upshock, but how this upshock is perceived was unknown. We found the vacuolar channel, Yvc1p, to be mechanosensitive, showing that the Ca2+ conduit is also the sensing molecule. Although fragile, the yeast vacuole allows limited direct mechanical examination. Pressures at tens of millimeters of Hg (1 mmHg = 133 Pa) activate the 400-pS Yvc1p conductance in whole-vacuole recording mode as well as in the excised cytoplasmic-side-out mode. Raising the bath osmolarity activates this channel and causes vacuolar shrinkage and deformation. It appears that, on upshock, a transient osmotic force activates Yvc1p to release Ca2+ from the vacuole. Mechanical activation of Yvc1p occurs regardless of Ca2+ concentration and is apparently independent of its known Ca2+ activation, which we now propose to be an amplification mechanism (Ca2+-induced Ca2+ release). Yvc1p is a member of the transient receptor potential-family channels, several of which have been associated with mechanosensation in animals. The possible use of Yvc1p as a molecular model to study mechanosensation in general is discussed.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1230540100