Subcellular localization and oligomeric structure of the yeast putative stretch-activated Ca2+ channel component Mid1
Abstract
The yeast Mid1 protein with an apparent molecular mass of 100 kDa is required for Ca2+ influx stimulated by the mating pheromone and by a capacitative calcium entrylike mechanism acting in response to Ca2+ depletion from the endoplasmic reticulum (ER) and functions as a stretch-activated Ca2+ -permeable channel when expressed in mammalian cells. Our previous work with protease protection experiments has indicated that Mid1 is present in the plasma membrane. In this study, we examined a possible intracellular localization of this protein by indirect fluorescence microscopy and found that Mid1 is present in the ER membrane as well as the plasma membrane. Intracellular fluorescence images for Mid1 were the same as those for the ER marker protein Sec71 but quite different from those of the Golgi protein Ypt1. The results were confirmed by membrane fractionation using Angiografin density gradient analysis. We also investigated the oligomeric structures and protein levels of Mid1 and found that Mid1 forms a 200-kDa oligomer by disulfide bonding. The protein level and modification of Mid1 in the plasma membrane and the ER membrane were unchanged by the mating pheromone. These findings provide new insight into the function of Mid1 in relation to localization, modification, and activation mechanisms.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Under nonreducing conditions, two distinct Mid1 protein bands were detected: a 100 kDa monomer and a 200 kDa likely complex.
“The 100 kDa band represented the Mid1 monomer, and the 200 kDa band likely corresponded to a Mid1 complex (Fig. 1C) (40).”
From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [40]
Mid1 likely forms an oligomer through sulfide bonding similar to Mid1 in yeast.
“This result suggested that Mid1 likely forms an oligomer through sulfide bonding similar to Mid1 in yeast (40).”
From Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress (2010) · cites this paper as [40]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works
Sikorski, R. S., & Hieter, P. (1989) · Genetics · doi:10.1093/genetics/122.1.19 · Cited by 8,685 · see citing works
Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,543 · see citing works
Jacob, H. (1988) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(88)80052-7 · Cited by 4,911 · see citing works
Gietz, R. D., & Sugino, A. (1988) · Gene · doi:10.1016/0378-1119(88)90185-0 · Cited by 2,901 · see citing works
Short protocols in molecular biology
(1996) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(97)80799-6 · Cited by 1,650 · see citing works
Molecular Basis of Mechanotransduction in Living Cells
Hamill, O. P., & Martinac, B. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.685 · Cited by 1,124 · see citing works
[40] Immunofluorescence methods for yeast
Pringle, J. R., Adams, A. E. M., Drubin, D. G., & Haarer, B. K. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94043-c · Cited by 704 · see citing works
Calcium/calmodulin-dependent and -independent phytochrome signal transduction pathways
Neuhaus, G., Bowler, C., Kern, R., & Chua, N. (1993) · Cell · doi:10.1016/0092-8674(93)90272-r · Cited by 473 · see citing works
MEC-2 regulates C. elegans DEG/ENaC channels needed for mechanosensation
Goodman, M. B., Ernstrom, G. G., Chelur, D. S., O’Hagan, R., Yao, C. A., & Chalfie, M. (2002) · Nature · doi:10.1038/4151039a · Cited by 321 · see citing works
MECHANOSENSITIVE CHANNELS OFESCHERICHIA COLI:The MscL Gene, Protein, and Activities
Sukharev, S., Blount, P., Martinac, B., & Kung, C. (1997) · Annual Review of Physiology · doi:10.1146/annurev.physiol.59.1.633 · Cited by 299 · see citing works
Essential role of calcineurin in response to endoplasmic reticulum stress
Bonilla, M., Nastase, K. K., & Cunningham, K. W. (2002) · The EMBO Journal · doi:10.1093/emboj/21.10.2343 · Cited by 255 · see citing works
MOLECULAR MODELING OF MECHANOTRANSDUCTION IN THE NEMATODE CAENORHABDITIS ELEGANS
Tavernarakis, N., & Driscoll, M. (1997) · Annual Review of Physiology · doi:10.1146/annurev.physiol.59.1.659 · Cited by 234 · see citing works
Review of Mechanosensitive Channels
Sackin, H. (1995) · Annual Review of Physiology · doi:10.1146/annurev.physiol.57.1.333 · Cited by 225 · see citing works
Iida, H., Yagawa, Y., & Anraku, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38311-5 · Cited by 224 · see citing works
Self-citationIida, H., Nakamura, H., Ono, T., Okumura, M. S., & Anraku, Y. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.8259 · Cited by 218 · see citing works
Self-citationMolecular Identification of a Eukaryotic, Stretch-Activated Nonselective Cation Channel
Kanzaki, M., Nagasawa, M., Kojima, I., Sato, C., Naruse, K., Sokabe, M., & Iida, H. (1999) · Science · doi:10.1126/science.285.5429.882 · Cited by 213 · see citing works
Self-citationCytoplasmic Free Ca2+ in Arabidopsis Roots Changes in Response to Touch but Not Gravity
Legué, V., Blancaflor, E. B., Wymer, C. L., Perbal, G., Fantin, D., & Gilroy, S. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.3.789 · Cited by 212 · see citing works
Locke, E. G., Bonilla, M., Liang, L., Takita, Y., & Cunningham, K. W. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6686-6694.2000 · Cited by 212 · see citing works
Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase
Iida, H., & Yahara, I. (1985) · Nature · doi:10.1038/315688a0 · Cited by 207 · see citing works
Self-citationSackin, H. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.002001 · Cited by 201 · see citing works
Paidhungat, M., & Garrett, S. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6339 · Cited by 191 · see citing works
The <i>Saccharomyces cerevisiae</i> CCH1 gene is involved in calcium influx and mating
Fischer, M., Schnell, N., Chattaway, J., Davies, P., Dixon, G., & Sanders, D. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01466-x · Cited by 185 · see citing works
French, A. S. (1992) · Annual Review of Physiology · doi:10.1146/annurev.ph.54.030192.001031 · Cited by 183 · see citing works
THE MOLECULES OF MECHANOSENSATION
Garcı́a-Añoveros, J., & Corey, D. P. (1997) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.20.1.567 · Cited by 177 · see citing works
The mechanosensory protein MEC-6 is a subunit of the C. elegans touch-cell degenerin channel
Chelur, D. S., Ernstrom, G. G., Goodman, M. B., Yao, C., Chen, L., O’Hagan, R., & Chalfie, M. (2002) · Nature · doi:10.1038/nature01205 · Cited by 164 · see citing works
Gehring, C., Williams, D. A., Cody, S. H., & Parish, R. W. (1990) · Nature · doi:10.1038/345528a0 · Cited by 158 · see citing works
Criado, M., & Keller, B. U. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80442-8 · Cited by 156 · see citing works
Matsumoto, T. K., Ellsmore, A. J., Cessna, S. G., Low, P. S., Pardo, J. M., Bressan, R. A., & Hasegawa, P. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205037200 · Cited by 155 · see citing works
Mediation of the Attachment or Fusion Step in Vesicular Transport by the GTP-Binding Ypt1 Protein
Segev, N. (1991) · Science · doi:10.1126/science.1904626 · Cited by 154 · see citing works
Klüsener, B., Boheim, G., Liss, H., Engelberth, J., & Weiler, E. W. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07271.x · Cited by 147 · see citing works
Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor.
Schandel, K. A., & Jenness, D. D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7245 · Cited by 143 · see citing works
Strayle, J., Pozzan, T., & Rudolph, H. K. (1999) · The EMBO Journal · doi:10.1093/emboj/18.17.4733 · Cited by 134 · see citing works
Muller, E. M., Locke, E., & Cunningham, K. W. (2001) · Genetics · doi:10.1093/genetics/159.4.1527 · Cited by 133 · see citing works
Nakajima‐Shimada, J., Iida, H., Tsuji, F. I., & Anraku, Y. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.15.6878 · Cited by 122 · see citing works
Self-citationRer1p as common machinery for the endoplasmic reticulum localization of membrane proteins
Sato, K., Sato, M., & Nakano, A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9693 · Cited by 104 · see citing works
Sato, K., Nishikawa, S., & Nakano, A. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.11.1459 · Cited by 104 · see citing works
Courchesne, W. E., & Ozturk, S. B. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03291.x · Cited by 79 · see citing works
Ohsumi, Y., & Anraku, Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85109-8 · Cited by 75 · see citing works
Single channel recordings of reconstituted ion channel proteins: an improved technique
Keller, B. U., Hedrich, R., Vaz, W. L. C., & Criado, M. (1988) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00581652 · Cited by 63 · see citing works
Erratum: corrigendum: MEC-2 regulates C. elegans DEG/ENaC channels needed for mechanosensation
Goodman, M. B., Ernstrom, G. G., Chelur, D. S., O’Hagan, R., Yao, C. A., & Chalfie, M. (2002) · Nature · doi:10.1038/nature00853 · Cited by 50 · see citing works
Kurihara, T., & Silver, P. A. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.9.919 · Cited by 45 · see citing works
Anion channels in giant liposomes made of endoplasmic reticulum vesicles from rat exocrine pancreas
Schmid, A., Gögelein, H., Kemmer, T. P., & Schulz, I. (1988) · The Journal of Membrane Biology · doi:10.1007/bf01872329 · Cited by 44 · see citing works
Tökés‐Füzesi, M., Bedwell, D. M., Repa, I., Sipos, K., Sümegi, B., Rab, A., & Miseta, A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02956.x · Cited by 40 · see citing works
Molecular Dissection of the Hydrophobic Segments H3 and H4 of the Yeast Ca2+ Channel Component Mid1
Tada, T., Ohmori, M., & Iida, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206993200 · Cited by 28 · see citing works
Self-citationEpitope mapping and accessibility of immunodominant regions of yeast plasma membrane H+‐ATPase
Serrano, R., Monk, B. C., Villalba, J. M., Montesinos, C., & Weiler, E. W. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17712.x · Cited by 28 · see citing works
Klüsener, B., Boheim, G., & Weiler, E. W. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00364-5 · Cited by 24 · see citing works
Wendt, M., & Sievers, A. (1989) · Plant and Cell Physiology · doi:10.1093/oxfordjournals.pcp.a077827 · Cited by 24 · see citing works
Transformation of Lithium-Treated Yeast Cells and the Selection of Auxotrophic and Dominant Markers
Mount, R. C., Jordan, B. E., & Hadfield, C. (2003) · Humana Press eBooks · doi:10.1385/0-89603-319-8:139 · Cited by 23 · see citing works
Maruoka, T., Nagasoe, Y., Inoue, S., Mori, Y., Goto, J., Ikeda, M., & Iida, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111603200 · Cited by 19 · see citing works
Self-citationKanzaki, M., Nagasawa, M., Kojima, I., Sato, C., Naruse, K., Sokabe, M., & Iida, H. (2000) · Science · doi:10.1126/science.288.5470.1347 · Cited by 18 · see citing works
Self-citation
Flagged first, then by citations
1 of the 55 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Nguyen, Q. B., Kadotani, N., Kasahara, S., Tosa, Y., MAYAMA, S., & Nakayashiki, H. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06242.x · Cited by 218 · see citing works
Leitz, G., Kang, B., Schoenwaelder, M. E. A., & Staehelin, L. A. (2009) · The Plant Cell · doi:10.1105/tpc.108.065052 · Cited by 182 · see citing works
Zelter, A., Benčina, M., Bowman, B. J., Yarden, O., & Read, N. D. (2004) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2004.05.001 · Cited by 129 · see citing works
Ihara‐Ohori, Y., Nagano, M., Muto, S., Uchimiya, H., & Kawai‐Yamada, M. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.090878 · Cited by 108 · see citing works
Lange, M., & Peiter, E. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.03100 · Cited by 90 · see citing works
Exogenous oxidative stress induces Ca2+ release in the yeast Saccharomyces cerevisiae
Popa, C., Dumitru, I., Ruta, L. L., Danet, A. F., & FARCASANU, I. C. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07794.x · Cited by 67 · see citing works
Kajiwara, K., Muneoka, T., Watanabe, Y., Karashima, T., Kitagaki, H., & Funato, K. (2012) · Molecular Microbiology · doi:10.1111/mmi.12056 · Cited by 62 · see citing works
Cch1 Restores Intracellular Ca2+ in Fungal Cells during Endoplasmic Reticulum Stress
Hong, M.-P., Vu, K., Bautos, J., & Gelli, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056218 · Cited by 54 · see citing works
Cavinder, B., Hamam, A. M., Lew, R. R., & Trail, F. (2011) · Eukaryotic Cell · doi:10.1128/ec.00235-10 · Cited by 53 · see citing works
Groppi, S., Belotti, F., Brandão, R. L., Martegani, E., & Tisi, R. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.03.006 · Cited by 49 · see citing works
Ancient association between cation leak channels and Mid1 proteins is conserved in fungi and animals
Ghezzi, A., Liebeskind, B. J., Thompson, A., Atkinson, N. S., & Zakon, H. H. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00015 · Cited by 40 · see citing works
A comparative genomic analysis of calcium and proton signaling/homeostasis in Aspergillus species
Benčina, M., Bagar, T., Lah, L., & Kraševec, N. (2009) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2008.07.019 · Cited by 38 · see citing works
Rigamonti, M., Groppi, S., Belotti, F., Ambrosini, R., Filippi, G., Martegani, E., & Tisi, R. (2015) · Cell Calcium · doi:10.1016/j.ceca.2014.12.003 · Cited by 34 · see citing works
Iida, K., Tada, T., & Iida, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.021 · Cited by 35 · see citing works
Self-citationSexual pheromone modulates the frequency of cytosolic Ca2+bursts inSaccharomyces cerevisiae
Carbó, N., Tarkowski, N., Ipiña, E. P., Dawson, S. P., & Aguilar, P. S. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-07-0481 · Cited by 34 · see citing works
Espeso, E. A. (2016) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-25304-6_7 · Cited by 33 · see citing works
Puigpinós, J., Casas, C., & Herrero, E. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1137 · Cited by 33 · see citing works
Harren, K., & Tudzynski, B. (2013) · Eukaryotic Cell · doi:10.1128/ec.00338-12 · Cited by 31 · see citing works
Yang, M., Brand, A., Srikantha, T., Daniels, K. J., Soll, D. R., & Gow, N. A. R. (2011) · Eukaryotic Cell · doi:10.1128/ec.00145-10 · Cited by 30 · see citing works
Clark, K. B. (2009) · Biosystems · doi:10.1016/j.biosystems.2009.08.005 · Cited by 25 · see citing works
Vlahakis, A., Muniozguren, N. L., & Powers, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201605030 · Cited by 25 · see citing works
Ca2+ homeostasis in the budding yeast Saccharomyces cerevisiae: Impact of ER/Golgi Ca2+ storage
D’hooge, P., Coun, C., Eyck, V. V., Faes, L., Ghillebert, R., Mariën, L., Winderickx, J., & Callewaert, G. (2015) · Cell Calcium · doi:10.1016/j.ceca.2015.05.004 · Cited by 25 · see citing works
Zhang, S., Zheng, H., Long, N., Carbó, N., Chen, P., Aguilar, P. S., & Lü, L. (2013) · Eukaryotic Cell · doi:10.1128/ec.00257-13 · Cited by 24 · see citing works
Hong, M.-P., Vu, K., Bautos, J. M., Tham, R. C., Jamklang, M., Uhrig, J. P., & Gelli, A. (2012) · Eukaryotic Cell · doi:10.1128/ec.00130-12 · Cited by 22 · see citing works
Ciliates learn to diagnose and correct classical error syndromes in mating strategies
Clark, K. B. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00229 · Cited by 21 · see citing works
Channeling Studies in Yeast: Yeast as a Model for Channelopathies?
Wolfe, D. M., & Pearce, D. A. (2006) · NeuroMolecular Medicine · doi:10.1385/nmm:8:3:279 · Cited by 18 · see citing works
宮脇, 千., Moriya, Y., Tatsumi, H., Iida, H., & Sokabe, M. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.08.014 · Cited by 17 · see citing works
Self-citationIida, K., Teng, J., Cho, T., Yoshikawa-Kimura, S., & Iida, H. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.810283 · Cited by 11 · see citing works
Self-citationKato, T., Kubo, A., Nagayama, T., Kume, S., Tanaka, C., Nakayama, Y., Iida, K., & Iida, H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181436 · Cited by 9 · see citing works
Self-citationLow, Y. S., Bircham, P. W., Maass, D. R., & Atkinson, P. H. (2014) · Molecular BioSystems · doi:10.1039/c3mb70414a · Cited by 8 · see citing works
Calcium Ion Channels in Saccharomyces cerevisiae
Dong, X. (2023) · Journal of Fungi · doi:10.3390/jof9050524 · Cited by 7 · see citing works
Coupling of a voltage‐gated Ca2+ channel homologue with a plasma membrane H+‐ATPase in yeast
Cho, T., Aya, I.-K., Fukata, Y., Nakayama, Y., Iida, K., Fukata, M., & Iida, H. (2016) · Genes to Cells · doi:10.1111/gtc.12458 · Cited by 7 · see citing works
Self-citationCalcium: a central player in Cryptococcus biology
Squizani, E. D., Reuwsaat, J. C. V., Motta, H., Tavanti, A. G., & Kmetzsch, L. (2021) · Fungal Biology Reviews · doi:10.1016/j.fbr.2021.03.004 · Cited by 8 · see citing works
Spolaor, S., Rovetta, M., Nobile, M. S., Cazzaniga, P., Tisi, R., & Besozzi, D. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.856030 · Cited by 7 · see citing works
Bioreaction Quantum Computing without Quantum Diffusion
Clark, K. B. (2012) · NeuroQuantology · doi:10.14704/nq.2012.10.4.574 · Cited by 7 · see citing works
With an Ear Up against the Wall: An Update on Mechanoperception in Arabidopsis
Behnami, S., & Bonetta, D. T. (2021) · Plants · doi:10.3390/plants10081587 · Cited by 6 · see citing works
Hayashi, T., Oishi, K., Kimura, M., Iida, K., & Iida, H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014378 · Cited by 5 · see citing works
Self-citationNoma, S., Iida, K., & Iida, H. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.8.1353-1363.2005 · Cited by 5 · see citing works
Self-citationTip Growth and Endocytosis in Fungi
Wendland, J., & Walther, A. (2005) · Springer eBooks · doi:10.1007/7089_018 · Cited by 4 · see citing works
Zanni, E., Franco, M., Nakano, M., Iida, H., Palleschi, C., & Uccelletti, D. (2012) · Microbiology · doi:10.1099/mic.0.056283-0 · Cited by 2 · see citing works
Self-citationRen, X., Wang, Y., Liu, Y., Tan, Y., Ren, C., Ge, Y., & Liu, Z. (2017) · Journal of Basic Microbiology · doi:10.1002/jobm.201700277 · Cited by 2 · see citing works
He, X., Tang, C., Wang, J., Subbarao, K. V., & Wang, Y. (2026) · aBIOTECH · doi:10.1016/j.abiote.2026.100076 · Cited by 2 · see citing works
(2004) · Yeast · doi:10.1002/yea.1091
- Authors
- Yoshimura, H., Tada, T., & Iida, H.
- Affiliations
- Tokyo Gakugei University (JP)
- Corresponding author
- Iida, Hidetoshi
- Venue
- Experimental Cell Research
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 293
- Issue
- 2
- Pages
- 185-195
- ISSN
- 0014-4827 (ISSN-L)
- OpenAlex
- W2078785949
- Cited by
- 45
- References
- 55
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 2 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 5 · 2013: 3 · 2012: 4
- FWCI
- 1.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- MID1, stretch-activated calcium channels, subcellular localization, oligomeric structure, disulfide bonds, endoplasmic reticulum membrane, plasma membrane, store-operated calcium entry, mating pheromone, yeast, Saccharomyces cerevisiae, protein modification
- MeSH terms
- Cell Membrane, Cells, Cultured, Disulfides, Endoplasmic Reticulum, Intracellular Membranes, Membrane Glycoproteins, Pheromones, Polymers, Saccharomyces cerevisiae, Calcium Channels, Calcium Signaling, rab GTP-Binding Proteins, Protein Structure, Quaternary, Saccharomyces cerevisiae Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review