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Nonetheless, 1 Microbial Senses and Ion Channels 15 Fig. 4 A cell-biological model of TRPY1 (Yvc1p) function. a The channel in the vacuolar membrane is closed when the cell is in an osmotic steady state. b A sudden increase in external osmolarity creates a disequilibrium. The evacuation of water (open arrows) causes the vacuole to shrink, deforming the vacuolar membrane. Local membrane stretch force generated by the deformation opens the TRPY1 channel, releasing Ca2+ into the cytoplasm (see Denis and Cyert 2002) Fig.

J. Haynes, unpublished results; Saimi et al. 2007). , although full-length TRPchannel genes have not been recognized or assembled from these genomes due to technical difficulties. To date, no experimental work has been reported on these putative TRP homologs in protists. The same search criterion revealed a TRP-channel gene in the genome of the budding yeast Saccharomyces cerevisiae, which has been experimentally studied at length (see below; Palmer et al. 2001; Zhou et al. 2003). By the criterion of sequence similarity to TM5-6, the yeast channel TRPY1 is more similar to animal TRPVs than animal TRPA, TRPC, TRPM, TRPP, TRPN, TRPML are to animal TRPVs.

3c). This observation was confirmed by others (Bihler et al. 2005) and this gene product was first named Yvc1, for yeast vacuolar channel (Palmer et al. 2001; Zhou et al. 2003), and later assigned as TRPY1 (Zhou et al. 2005) since it is a TRP homolog. This identification of TRPY1 took this vacuolar channel beyond biophysical description into the realm of cell and molecular biology. The first finding on the cell-biological significance of TRPY1 was made in the Cyert laboratory (Denis and Cyert 2002).

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