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A Homolog of Mammalian, Voltage-Gated Calcium Channels Mediates Yeast Pheromone-Stimulated Ca 2+ Uptake and Exacerbates the cdc1 (Ts) Growth Defect
Open accessAbstract
Previous studies attributed the yeast (Saccharomyces cerevisiae) cdc1(Ts) growth defect to loss of an Mn2+-dependent function. In this report we show that cdc1(Ts) temperature-sensitive growth is also associated with an increase in cytosolic Ca2+. We identified two recessive suppressors of the cdc1(Ts) temperature-sensitive growth which block Ca2+ uptake and accumulation, suggesting that cytosolic Ca2+ exacerbates or is responsible for the cdc1(Ts) growth defect. One of the cdc1(Ts) suppressors is identical to a gene, MID1, recently implicated in mating pheromone-stimulated Ca2+ uptake. The gene (CCH1) corresponding to the second suppressor encodes a protein that bears significant sequence similarity to the pore-forming subunit (alpha1) of plasma membrane, voltage-gated Ca2+ channels from higher eukaryotes. Strains lacking Mid1 or Cch1 protein exhibit a defect in pheromone-induced Ca2+ uptake and consequently lose viability upon mating arrest. The mid1delta and cch1delta mutants also display reduced tolerance to monovalent cations such as Li+, suggesting a role for Ca2+ uptake in the calcineurin-dependent ion stress response. Finally, mid1delta cch1delta double mutants are, by both physiological and genetic criteria, identical to single mutants. These and other results suggest Mid1 and Cch1 are components of a yeast Ca2+ channel that may mediate Ca2+ uptake in response to mating pheromone, salt stress, and Mn2+ depletion.
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“Unfortunately, the measurement of Cch1 channel activity in a heterologous expression system had been impossible until recently because of the significant challenge posed by the molecular cloning of CCH1 as a result of the toxicity of the CCH1 gene or gene product in Escherichia coli cells (8).”
From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [8]
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“Three new Ca2 channel proteins, which have close homologues to the three Ca2 channel proteins (Mid1p, Cch1p, and Yvc1p [238, 545, 583]) in S. cerevisiae, have been identified in Neurospora.”
Background
Metadata
- Authors
- Paidhungat, M., & Garrett, S.
- Affiliations
- Duke University (US)
- ORCID
- Garrett, Stephen
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1997-11
- Volume
- 17
- Issue
- 11
- Pages
- 6339-6347
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC232485
- OpenAlex
- W2162829341
- Cited by
- 191
- References
- 40
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 11 · 2016: 9 · 2015: 6 · 2014: 8 · 2013: 8 · 2012: 12
- FWCI
- 2.02
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- voltage-gated calcium channels, calcium uptake, MID1, mating pheromone signaling, intracellular calcium, lithium tolerance, manganese depletion, salt stress, Saccharomyces cerevisiae
- MeSH terms
- Amino Acid Sequence, Biological Transport, Calcium, Fungal Proteins, Membrane Glycoproteins, Molecular Sequence Data, Mutation, Pheromones, Saccharomyces cerevisiae, Suppression, Genetic, Calcium Channels, Ion Channel Gating, Gene Expression, Sequence Homology, Amino Acid, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins
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