The transient receptor potential channel on the yeast vacuole is  mechanosensitive

Zhou, Xian; Batiza, Ann; Loukin, Stephen H.; Palmer, Chris P.; Kung, Ching; Saimi, Yoshiro

doi:10.1073/pnas.1230540100

Cited by 145 publications

(127 citation statements)

References 49 publications

(62 reference statements)

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“…The recently identified yeast transient receptor potential channel homologue, Yvc1p, was shown to localize to the vacuolar membrane and mediate Ca 2ϩ efflux out of the vacuole (10). Additional reports have shown that vacuolar Ca 2ϩ efflux by Yvc1p can be specifically induced by hypotonic shock, which may be mediated by a mechano-sensitive mechanism (11,12).…”

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confidence: 99%

The Ca2+ Homeostasis Defects in a pgm2Δ Strain of Saccharomyces cerevisiae Are Caused by Excessive Vacuolar Ca2+ Uptake Mediated by the Ca2+-ATPase Pmc1p

Aiello

Miseta³

et al. 2004

Journal of Biological Chemistry

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Loss of the major isoform of phosphoglucomutase (PGM) causes an accumulation of glucose 1-phosphate when yeast cells are grown with galactose as the carbon and energy source. Remarkably, the pgm2⌬ strain also exhibits a severe imbalance in intracellular Ca 2؉ homeostasis when grown under these conditions. In the present study, we examined how the pgm2⌬ mutation alters yeast Ca 2؉ homeostasis in greater detail. We found that a shift from glucose to galactose as the carbon source resulted in a 2-fold increase in the rate of cellular Ca 2؉ uptake in wild-type cells, whereas Ca 2؉ uptake increased 8-fold in the pgm2⌬ mutant. Disruption of the PMC1 gene, which encodes the vacuolar Ca 2؉ -ATPase Pmc1p, suppressed the Ca 2؉ -related phenotypes observed in the pgm2⌬ strain. This suggests that excessive vacuolar Ca 2؉ uptake is tightly coupled to these defects in Ca 2؉ homeostasis. An in vitro assay designed to measure Ca 2؉ sequestration into intracellular compartments confirmed that the pgm2⌬ mutant contained a higher level of Pmc1p-dependent Ca 2؉ transport activity than the wild-type strain. We found that this increased rate of vacuolar Ca 2؉ uptake also coincided with a large induction of the unfolded protein response in the pgm2⌬ mutant, suggesting that Ca 2؉ uptake into the endoplasmic reticulum compartment was reduced. These results indicate that the excessive Ca 2؉ uptake and accumulation previously shown to be associated with the pgm2⌬ mutation are due to a severe imbalance in the distribution of cellular Ca 2؉ into different intracellular compartments.

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confidence: 99%

The Ca2+ Homeostasis Defects in a pgm2Δ Strain of Saccharomyces cerevisiae Are Caused by Excessive Vacuolar Ca2+ Uptake Mediated by the Ca2+-ATPase Pmc1p

Aiello

Miseta³

et al. 2004

Journal of Biological Chemistry

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“…Corresponding to this role in vivo, TRPY1 was found to be mechanosensitive under patch clamp (13). Like its counterparts in animals, TRPY1 is polymodal and also can be activated by cytoplasmic Ca 2ϩ , likely amplifying its own activation through a Ca 2ϩ -induced Ca 2ϩ -release feedback (13).…”

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confidence: 99%

Yeast gain-of-function mutations reveal structure–function relationships conserved among different subfamilies of transient receptor potential channels

Su¹,

Zhou²,

Haynes³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…A TRP channel (TrpY1) is present in the vacuolar membrane of yeast and functions as a mechanosensitive channel (7,8). The finding that TrpY1 releases Ca 2ϩ upon hyperosmotic shock suggests that this intracellular mechanosensitive channel responds to environmental stress.…”

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confidence: 99%

Molecular and electrophysiological characterization of a mechanosensitive channel expressed in the chloroplasts of Chlamydomonas

Nakayama

Fujiu

Sokabe

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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MscS is a mechanosensitive channel that is ubiquitous among bacteria. Recent progress in the genome projects has revealed that homologs of MscS are also present in eukaryotes, but whether they operate as ion channels is unknown. In this study we cloned MSC1, a homolog of MscS in Chlamydomonas, and examined its function when expressed in Escherichia coli. Full-length MSC1 was not functional when expressed in E. coli cells. However, removal of the N-terminal signal sequence (⌬N-MSC1) reversed this effect. ⌬N-MSC1 was found to open in response to membrane stretch and displayed a preference for anions over cations as permeable ions. ⌬N-MSC1 exhibited marked hysteretic behavior in response to ascending and descending stimuli. That is, channel gating occurred in response to significant stimuli but remained open until the stimulus was almost completely removed. Indirect immunofluorescence revealed that MSC1 is present as punctate spots in the cytoplasm and chloroplasts. Moreover, knockdown of MSC1 expression resulted in the abnormal localization of chlorophyll. These findings show that MSC1 is an intracellular mechanosensitive channel and is responsible for the organization of chloroplast in Chlamydomonas.MscS ͉ hysteresis ͉ heterogeneous expression ͉ knockdown ͉ green algae M echanosensation is typically involved in auditory perception, touch sensation, proprioception, and gravity perception. The mechanoreceptor potential in sensory cells is mediated by mechanosensitive channels, which are activated by stretching or deformation of the membrane. The patch-clamp technique has revealed that mechanosensitive channels are present in almost every cell type, not just sensory cells. In fact, mechanosensitive channels were first recorded with the patch-clamp method in the muscle cell (1). Mechanosensitive channels in nonsensory cells are believed to be responsible for monitoring cell deformation evoked by contact with surrounding materials and by changes in osmolarity.Bacteria harbor the mechanosensitive channels MscS and MscL, which act to protect against hypoosmotic downshock (2). The presence of MscS homologs in virtually all eubacteria and archaea suggests that MscS has an essential function in prokaryotes, but whether every MscS homolog serves as a mechanosensitive channel is uncertain. For instance, although there are at least six MscS homologs in the Escherichia coli genome, only two of them (MscS and MscK) have been detected by electrophysiological methods (3, 4). Recent genomic projects on eukaryotes have uncovered the presence of MscS homologs in some plants (Arabidopsis and Oryza), protists (Chlamydomonas), and fungi (Schizosaccharomyces). Curiously, MscS homologs have not been found in animals (5, 6). The MscS homologs of Arabidopsis (MSL2 and MSL3) have been observed as one or two foci on the plastid envelope, and their double knockout results in an abnormal size and shape of the plastids (6). This finding suggests that one of the possible functions of the MscS homologs is to control the size and shape of the intr...

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The transient receptor potential channel on the yeast vacuole is mechanosensitive

Cited by 145 publications

References 49 publications

The Ca2+ Homeostasis Defects in a pgm2Δ Strain of Saccharomyces cerevisiae Are Caused by Excessive Vacuolar Ca2+ Uptake Mediated by the Ca2+-ATPase Pmc1p

The Ca2+ Homeostasis Defects in a pgm2Δ Strain of Saccharomyces cerevisiae Are Caused by Excessive Vacuolar Ca2+ Uptake Mediated by the Ca2+-ATPase Pmc1p

Yeast gain-of-function mutations reveal structure–function relationships conserved among different subfamilies of transient receptor potential channels

Molecular and electrophysiological characterization of a mechanosensitive channel expressed in the chloroplasts of Chlamydomonas

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