Cited by 213Ion channel regulation and functionIon Channels and ReceptorsErythrocyte Function and Pathophysiology

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Molecular Identification of a Eukaryotic, Stretch-Activated Nonselective Cation Channel

Kanzaki, Makoto, Nagasawa, Masahiro, Kojima, Itaru, Sato, Chikara, Naruse, Keiji, Sokabe, Masahiro, Iida, Hidetoshi·1999·Science

DOI 10.1126/science.285.5429.882

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Abstract

Calcium-permeable, stretch-activated nonselective cation (SA Cat) channels mediate cellular responses to mechanical stimuli. However, genes encoding such channels have not been identified in eukaryotes. The yeast MID1 gene product (Mid1) is required for calcium influx in the yeast Saccharomyces cerevisiae . Functional expression of Mid1 in Chinese hamster ovary cells conferred sensitivity to mechanical stress that resulted in increases in both calcium conductance and the concentration of cytosolic free calcium. These increases were dependent on the presence of extracellular calcium and were reduced by gadolinium, a blocker of SA Cat channels. Single-channel analyses with cell-attached patches revealed that Mid1 acts as a calcium-permeable, cation-selective stretch-activated channel with a conductance of 32 picosiemens at 150 millimolar cesium chloride in the pipette. Thus, Mid1 appears to be a eukaryotic, SA Cat channel.

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Nakajima‐Shimada, J., Sakaguchi, S., Tsuji, F. I., Anraku, Y., & Iida, H. (2000) · Cell Structure and Function · doi:10.1247/csf.25.125 · Cited by 11
“The MID1 gene encodes a stretch-activated cation channel required for Ca2+ influx and mating (Iida et al., 1994; Kanzaki et al., 1999).”
BackgroundSelf-citation
Optimized Heart Failure Therapy and Complete Anemia Correction on Left-Ventricular Hypertrophy in Nondiabetic and Diabetic Patients Undergoing Hemodialysis
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Cytotoxicity of Oleandrin Is Mediated by Calcium Influx and by Increased Manganese Uptake in Saccharomyces cerevisiae Cells
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“Since Mid1 is a stretch-activated Ca2+-permeable cation channel [58], it is possible that oleandrin activates it by”
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MID1-COMPLEMENTING ACTIVITY regulates cell proliferation and development via Ca2+ signaling in Marchantia polymorpha
Iwano, M., Suetsugu, N., Nishihama, R., Ishida, S., Horie, T., Costa, A., Katsuno, T., Kimura, M., Iida, K., Iida, H., et al. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae613 · Cited by 11
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PpMID1 Plays a Role in the Asexual Development and Virulence of Phytophthora parasitica
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“cerevisiae MID1 contains an ORF of 548 aa and alone is capable of forming a calciumpermeable, cation-selective stretch-activated channel in Chinese hamster ovary cells (Kanzaki et al., 1999).”
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“Mechanoreceptors (mechanosensitive ion channels) are present on the plasma membrane of plants, as of other organisms (Kanzaki et al., 1999; Nakagawa et al., 2007).”
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“(VDCC) (Fischer et al. 1997) and/or MID1, a mechanosensitive nonselective cation channel (MSCC) ( Kanzaki et al. 1999 ), are not capable of growth and survival in synthetic medium with lowered Ca 2+ concentration.”
BackgroundSelf-citation
Current status of temporomandibular joint disorders and the therapeutic system derived from a series of biomechanical, histological, and biochemical studies
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“On the other hand, mechanoreceptors (mechanosensitive ion channels) are present in various organisms, including plants, on the plasma membrane (Kanzaki et al., 1999; Nakagawa et al., 2007).”
Background
Strain-induced mechanoresponse depends on cell contractility and BAG3-mediated autophagy
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“…of strain sensing and subsequent signal transduction depend on multiple elementary processes, including mechanically activated ion channels, tension-dependent conformational changes of proteins, and tension-dependent binding affinities (Kanzaki et al. , 1999; Hayakawa et al. , 2008, 2011).”
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“The proposal that Mid1 was that channel protein ( Kanzaki et al. 1999 ) was not substantiated, since mid1∆ yeast retains 36-pS mechanosensitive conductance (X.-L.”
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A New Insight into the Function of TRPV2 in Circulatory Organs
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Self-citation
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Polarized Morphogenesis Regulator Spa2 Is Required for the Function of Putative Stretch-Activated Ca 2+ -Permeable Channel Component Mid1 in Saccharomyces cerevisiae
Noma, S., Iida, K., & Iida, H. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.8.1353-1363.2005 · Cited by 5
Self-citation
Calcium Signaling Networks in Yeast
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Involvement of MID1-COMPLEMENTING ACTIVITY 1 encoding a mechanosensitive ion channel in prehaustorium development of the stem parasitic plant Cuscuta campestris
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“This mutant exhibits reduced viability in the presence of the mating pheromone, α -factor (Iida et al. 1994, Kanzaki et al. 1999).”
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Phe356 in the yeast Ca2+ channel component Mid1 is a key residue for viability after exposure to α-factor
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Calcium homeostasis plays important roles in the internalization and activities of the small synthetic antifungal peptide PAF26
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Authors: Kanzaki, M., Nagasawa, M., Kojima, I., Sato, C., Naruse, K., Sokabe, M., & Iida, H.
Affiliations: Gunma University (JP)
Supermolecular Science Division, Electrotechnical Laboratory, Tsukuba, Ibaraki 305-8568, Japan.
Nagoya University (JP)
Tokyo Gakugei University (JP)
Corresponding author: Iida, Hidetoshi
ORCID: Kanzaki, Makoto
Kojima, Itaru
Sato, Chikara
Naruse, Keiji
Sokabe, Masahiro
Iida, Hidetoshi
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1999-08-06
Volume: 285
Issue: 5429
Pages: 882-886
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.285.5429.882
OpenAlex: W2026402396
Cited by: 213
References: 23
Citations by year: 2025: 2 · 2024: 3 · 2022: 4 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 7 · 2014: 9 · 2013: 9 · 2012: 9
FWCI: 5.05
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Health Sciences › Medicine › Physiology (medical) › Erythrocyte Function and Pathophysiology
Keywords: stretch-activated channels, non-selective cation channels, calcium-permeable channels, MID1, Saccharomyces cerevisiae, mechanical stress, calcium influx, gadolinium, single-channel conductance, cation selectivity, cytosolic free calcium
MeSH terms: Amino Acid Sequence, Animals, Calcium, Cations, Cell Membrane, Cell Membrane Permeability, Cesium, Chlorides, Fungal Proteins, Gadolinium, Cricetinae, Ion Channels, Membrane Glycoproteins, Membrane Potentials, Molecular Sequence Data, Pressure, Saccharomyces cerevisiae, Stress, Mechanical, Transfection, Calcium Channels, CHO Cells, Zinc Compounds, Patch-Clamp Techniques, Saccharomyces cerevisiae Proteins

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Molecular Identification of a Eukaryotic, Stretch-Activated Nonselective Cation Channel

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