The phosphoinositide 3-kinase regulates retrograde trafficking of the iron permease CgFtr1 and iron homeostasis in Candida glabrata
Open accessAbstract
The phosphoinositide 3-kinase (PI3K), which phosphorylates phosphatidylinositol and produces PI3P, has been implicated in protein trafficking, intracellular survival, and virulence in the pathogenic yeast Candida glabrata Here, we demonstrate PI3-kinase (CgVps34) to be essential for maintenance of cellular iron homeostasis. We examine how CgVps34 regulates the fundamental process of iron acquisition, and underscore its function in vesicular trafficking as a central determinant. RNA sequencing analysis revealed iron homeostasis genes to be differentially expressed upon CgVps34 disruption. Consistently, the Cgvps34Δ mutant displayed growth attenuation in low- and high-iron media, increased intracellular iron content, elevated mitochondrial aconitase activity, impaired biofilm formation, and extenuated mouse organ colonization potential. Furthermore, we demonstrate for the first time that C. glabrata cells respond to iron limitation by expressing the iron permease CgFtr1 primarily on the cell membrane, and to iron excess via internalization of the plasma membrane-localized CgFtr1 to the vacuole. Our data show that CgVps34 is essential for the latter process. We also report that macrophage-internalized C. glabrata cells express CgFtr1 on the cell membrane indicative of an iron-restricted macrophage internal milieu, and Cgvps34Δ cells display better survival in iron-enriched medium-cultured macrophages. Overall, our data reveal the centrality of PI3K signaling in iron metabolism and host colonization.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The ability of C. glabrata to form biofilms is enhanced in the high-iron environment.
“The ability of C. glabrata to form biofilms has also been found to be enhanced in the high-iron environment [57].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [57]
There is a close association between the capacity to form biofilms and colonize murine organs in the systemic candidiasis model.
“Moreover, recent studies have shown a close association between the capacity to form biofilms and colonize murine organs in the systemic candidiasis model [57,58], however, the precise mechanisms underlying this relationship are unknown.”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [57]
Retrograde trafficking of CgFtr1 from the plasma membrane to the vacuole is dependent on the sole class III phosphoinositide 3-kinase kinase CgVps34.
“This retrograde trafficking of CgFtr1 from the plasma membrane to the vacuole is dependent on the sole class III phosphoinositide 3-kinase kinase, CgVps34 [57].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [57]
C. glabrata responds to iron-deplete conditions via expression of the high-affinity iron permease CgFtr1 on the plasma membrane.
“Furthermore, C. glabrata has been reported to respond to iron-deplete condition via expression of the high-affinity iron permease CgFtr1 on the plasma membrane, and to iron-replete condition by trafficking CgFtr1 to the vacuole [57].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [57]
C. glabrata responds to iron-replete conditions by trafficking CgFtr1 to the vacuole.
“Furthermore, C. glabrata has been reported to respond to iron-deplete condition via expression of the high-affinity iron permease CgFtr1 on the plasma membrane, and to iron-replete condition by trafficking CgFtr1 to the vacuole [57].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [57]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Trapnell, C., Williams, B. A., Pertea, G., Mortazavi, A., Kwan, G., van Baren, M. J., Salzberg, S. L., Wold, B. J., & Pachter, L. (2010) · Nature Biotechnology · doi:10.1038/nbt.1621 · Cited by 15,556 · see citing works
Hidden Killers: Human Fungal Infections
Brown, G. D., Denning, D. W., Gow, N. A. R., Levitz, S. M., Netea, M. G., & White, T. C. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004404 · Cited by 4,284 · see citing works
Epidemiology of Invasive Candidiasis: a Persistent Public Health Problem
Pfaller, M. A., & Diekema, D. J. (2007) · Clinical Microbiology Reviews · doi:10.1128/cmr.00029-06 · Cited by 4,174 · see citing works
Nutritional immunity: transition metals at the pathogen–host interface
Hood, M. I., & Skaar, E. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2836 · Cited by 1,535 · see citing works
Iron in infection and immunity
Cassat, J. E., & Skaar, E. P. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.010 · Cited by 1,214 · see citing works
Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J. F., & Waterfield, M. D. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.615 · Cited by 1,204 · see citing works
PI3K signalling: the path to discovery and understanding
Vanhaesebroeck, B., Stephens, L., & Hawkins, P. T. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3290 · Cited by 991 · see citing works
Macrophage defense mechanisms against intracellular bacteria
Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · see citing works
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works
Fidel, P. L., Vazquez, J. A., & Sobel, J. D. (1999) · Clinical Microbiology Reviews · doi:10.1128/cmr.12.1.80 · Cited by 953 · see citing works
The fungal vacuole: composition, function, and biogenesis
Klionsky, D. J., Herman, P. K., & Emr, S. D. (1990) · Microbiological Reviews · doi:10.1128/mr.54.3.266-292.1990 · Cited by 781 · see citing works
A permease-oxidase complex involved in high-affinity iron uptake in yeast.
Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., Klausner, R. D., & Dancis, A. (1996) · Science · doi:10.1126/science.271.5255.1552 · Cited by 683 · see citing works
The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.
Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670 · see citing works
The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 501 · see citing works
Solubility of lead, zinc and copper added to mineral soils
Martı́nez, C. E., & Motto, H. L. (2000) · Environmental Pollution · doi:10.1016/s0269-7491(99)00111-6 · Cited by 483 · see citing works
Fanning, S., & Mitchell, A. P. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002585 · Cited by 465 · see citing works
The yeast lysosome-like vacuole: Endpoint and crossroads
Li, S. C., & Kane, P. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.08.003 · Cited by 453 · see citing works
Invasive Fungal Pathogens: Current Epidemiological Trends
Pfaller, M. A., Pappas, P. G., & Wingard, J. R. (2006) · Clinical Infectious Diseases · doi:10.1086/504490 · Cited by 448 · see citing works
Genetic Basis of Mitochondrial Function and Morphology in Saccharomyces cerevisiae
Dimmer, K. S., Fritz, S., Fuchs, F., Messerschmitt, M., Weinbach, N., Neupert, W., & Westermann, B. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0588 · Cited by 443 · see citing works
Pfaller, M. A., Neofytos, D., Diekema, D. J., Azie, N. E., Meier‐Kriesche, H., Quan, S.-P., & Horn, D. (2012) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2012.10.003 · Cited by 391 · see citing works
Cormack, B. P., Ghori, N., & Falkow, S. (1999) · Science · doi:10.1126/science.285.5427.578 · Cited by 383 · see citing works
Classes of phosphoinositide 3-kinases at a glance
Jean, S., & Kiger, A. A. (2014) · Journal of Cell Science · doi:10.1242/jcs.093773 · Cited by 380 · see citing works
Almeida, R. S., Brunke, S., Albrecht, A., Thewes, S., Laue, M., Edwards, J. E., Filler, S. G., & Hube, B. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000217 · Cited by 330 · see citing works
The FET4 gene encodes the low affinity Fe(II) transport protein of Saccharomyces cerevisiae
Dix, D., Bridgham, J. T., Broderius, M. A., Byersdorfer, C. A., & Eide, D. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47163-3 · Cited by 320 · see citing works
The French Mycosis Study Group, Lortholary, O., Renaudat, C., Sitbon, K., Madec, Y., Denoeud‐Ndam, L., Wolff, M., Fontanet, A. L., Bretagne, S., & Dromer, F. (2014) · Intensive Care Medicine · doi:10.1007/s00134-014-3408-3 · Cited by 310 · see citing works
A yeast by any other name: Candida glabrata and its interaction with the host
Kaur, R., Domergue, R., Zupancic, M. L., & Cormack, B. P. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.06.012 · Cited by 271 · see citing works
Self-citationIsolation of Yeast Mitochondria
Meisinger, C., Pfanner, N., & Truscott, K. N. (2005) · Humana Press eBooks · doi:10.1385/1-59259-958-3:033 · Cited by 270 · see citing works
Candida glabrata: A review of its features and resistance
Rodrigues, C. F., Silva, S., & Henriques, M. (2014) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-013-2009-3 · Cited by 268 · see citing works
De Las Peñas, A., Pan, S.-J., Castaño, I., Alder, J., Cregg, R., & Cormack, B. P. (2003) · Genes & Development · doi:10.1101/gad.1121003 · Cited by 268 · see citing works
Regulation of Cation Balance inSaccharomyces cerevisiae
Cyert, M., & Philpott, C. C. (2013) · Genetics · doi:10.1534/genetics.112.147207 · Cited by 253 · see citing works
Silva, D. M. D., Askwith, C. C., Eide, D. J., & Kaplan, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1098 · Cited by 246 · see citing works
Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria
Bulteau, A.-L., Ikeda-Saito, M., & Szweda, L. I. (2003) · Biochemistry · doi:10.1021/bi0353979 · Cited by 241 · see citing works
Transition Metal Transport in Yeast
Ho, A. V., Ward, D. M., & Kaplan, J. (2002) · Annual Review of Microbiology · doi:10.1146/annurev.micro.56.012302.160847 · Cited by 225 · see citing works
Burda, P., Padilla, S. M., Sarkar, S., & Emr, S. D. (2002) · Journal of Cell Science · doi:10.1242/jcs.00090 · Cited by 216 · see citing works
Shingu-Vazquez, M., & Traven, A. (2011) · Eukaryotic Cell · doi:10.1128/ec.05184-11 · Cited by 209 · see citing works
Schwarzmüller, T., Ma, B., Hiller, E., Istel, F., Tscherner, M., Brunke, S., Ames, L., Firon, A., Green, B., Cabral, V., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004211 · Cited by 191 · see citing works
Abe, F., & Hiraki, T. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.12.002 · Cited by 181 · see citing works
Ramírez, M. A., & Lorenz, M. C. (2007) · Eukaryotic Cell · doi:10.1128/ec.00372-06 · Cited by 174 · see citing works
Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling
Strochlic, T. I., Setty, T. G., Sitaram, A., & Burd, C. G. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609161 · Cited by 166 · see citing works
Yeast, a model organism for iron and copper metabolism studies
Freitas, J. M. D., Henri Wintz, A., Kim, J. H., Poynton, H. C., Fox, T. C., & Vulpe, C. D. (2003) · BioMetals · doi:10.1023/a:1020771000746 · Cited by 164 · see citing works
Frieman, M., McCaffery, J. M., & Cormack, B. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03166.x · Cited by 159 · see citing works
Roetzer, A., Gabaldón, T., & Schüller, C. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2010.02102.x · Cited by 154 · see citing works
Ramsay, L. M., & Gadd, G. M. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1997.tb10442.x · Cited by 150 · see citing works
Tortorano, A. M., Dho, G., Prigitano, A., Breda, G., Grancini, A., Emmi, V., Cavanna, C., Marino, G., Morero, S., Ossi, C. M., et al. (2011) · Mycoses · doi:10.1111/j.1439-0507.2011.02044.x · Cited by 142 · see citing works
Crusade for iron: iron uptake in unicellular eukaryotes and its significance for virulence
Šuťák, R., Lesuisse, E., Tachezy, J., & Richardson, D. R. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.03.005 · Cited by 142 · see citing works
Serrano, R., Bernal, D., Simón, E., & Ariño, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313746200 · Cited by 136 · see citing works
Rai, M. N., Balusu, S., Gorityala, N., Dandu, L., & Kaur, R. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002863 · Cited by 117 · see citing works
Self-citationJohnson, M., Cockayne, A., Williams, P. H., & Morrissey, J. A. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.23.8211-8215.2005 · Cited by 117 · see citing works
Mobilization of Stored Iron in Mammals: A Review
Linder, M. C. (2013) · Nutrients · doi:10.3390/nu5104022 · Cited by 111 · see citing works
Candida albicans specializations for iron homeostasis: from commensalism to virulence
Noble, S. M. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.09.006 · Cited by 104 · see citing works
The long physiological reach of the yeast vacuolar H+-ATPase
Kane, P. M. (2007) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-007-9112-z · Cited by 103 · see citing works
Gabaldón, T., & Carreté, L. (2016) · FEMS Yeast Research · doi:10.1093/femsyr/fov110 · Cited by 99 · see citing works
Post-transcriptional Regulation of the Yeast High Affinity Iron Transport System
Felice, M. R., Domenico, I. D., Li, L., Ward, D. M., Bartók, B., Musci, G., & Kaplan, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414663200 · Cited by 98 · see citing works
Nevitt, T., & Thiele, D. J. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001322 · Cited by 95 · cited 2× · see citing works
“glabrata neither synthesizes nor secretes high-affinity ironchelating compounds, siderophores, it does possess the sole siderophore transporter, CgSit1, which is essential for utilization of ferrichrome as an iron source under iron-deficient conditions, and for iron-dependent survival in macrophages (10, 18).”
BackgroundExpression Plasmids for Use inCandida glabrata
Zordan, R. E., Yuxia, R., Pan, S., Rotondo, G., Peñas, A. D. L., Iluore, J., & Cormack, B. P. (2013) · G3 Genes Genomes Genetics · doi:10.1534/g3.113.006908 · Cited by 82 · see citing works
Strochlic, T. I., Schmiedekamp, B. C., Lee, J. R. E., Katzmann, D. J., & Burd, C. G. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-03-0296 · Cited by 75 · see citing works
Singh, A., Severance, S., Kaur, N., Wiltsie, W., & Kosman, D. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512042200 · Cited by 74 · see citing works
Srivastava, V. K., Suneetha, K. J., & Kaur, R. (2014) · Biochemical Journal · doi:10.1042/bj20140598 · Cited by 69 · see citing works
Self-citationBairwa, G., Rasheed, M., Taigwal, R., Sahoo, R., & Kaur, R. (2014) · Biochemical Journal · doi:10.1042/bj20130757 · Cited by 36 · see citing works
Srivastava, V. K., Suneetha, K. J., & Kaur, R. (2015) · The FEBS Journal · doi:10.1111/febs.13264 · Cited by 33 · see citing works
Self-citationRai, M. N., Sharma, V., Balusu, S., & Kaur, R. (2014) · Cellular Microbiology · doi:10.1111/cmi.12364 · Cited by 27 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Iron acquisition in fungal pathogens of humans
Bairwa, G., Jung, W. H., & Kronstad, J. W. (2017) · Metallomics · doi:10.1039/c6mt00301j · Cited by 151 · see citing works
Candida glabrata: A Lot More Than Meets the Eye
Kumar, K., Askari, F., Sahu, M. S., & Kaur, R. (2019) · Microorganisms · doi:10.3390/microorganisms7020039 · Cited by 128 · see citing works
Self-citationDivergent Approaches to Virulence in C. albicans and C. glabrata: Two Sides of the Same Coin
Galocha, M., Pais, P., Cavalheiro, M., Pereira, D., Viana, R., & Teixeira, M. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092345 · Cited by 105 · see citing works
Adaptation to iron deficiency in human pathogenic fungi
Martínez‐Pastor, M. T., & Puig, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118797 · Cited by 46 · see citing works
Gerwien, F., Safyan, A., Wisgott, S., Brunke, S., Kasper, L., & Hube, B. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01055 · Cited by 33 · see citing works
Synthesis and in vitro anti-bladder cancer activity evaluation of quinazolinyl-arylurea derivatives
Chen, J.-N., Li, T., Cheng, L., Qin, T.-S., Sun, Y., Chen, C.-T., He, Y., Liu, G., Yao, D., Wei, Y., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112661 · Cited by 33 · see citing works
The regulation of iron homeostasis in the fungal human pathogen Candida glabrata
Devaux, F., & Thiébaut, A. (2019) · Microbiology · doi:10.1099/mic.0.000807 · Cited by 29 · see citing works
Candida glabrata is a successful pathogen: An artist manipulating the immune response
Castrejón-Jiménez, N. S., Castillo-Cruz, J., Baltierra‐Uribe, S. L., Hernández-González, J. C., & Estela, G.-P. B. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127038 · Cited by 28 · see citing works
“We've got to get out”—Strategies of human pathogenic fungi to escape from phagocytes
Sonnberger, J., Kasper, L., Lange, T., Brunke, S., & Hube, B. (2023) · Molecular Microbiology · doi:10.1111/mmi.15149 · Cited by 14 · see citing works
An iron-dependent metabolic vulnerability underlies VPS34-dependence in RKO cancer cells
Kobylarz, M. J., Goodwin, J. M., Kang, Z. B., Annand, J. W., Hevi, S., O’Mahony, E., McAllister, G., Reece-Hoyes, J. S., Wang, Q., Alford, J., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235551 · Cited by 14 · see citing works
Eliaš, D., Hervay, N. T., Bujdoš, M., & Gbelská, Y. (2023) · Journal of Fungi · doi:10.3390/jof9050579 · Cited by 12 · see citing works
Denecker, T., Li, Y. Z., Fairhead, C., Budin, K., Camadro, J., Bolotin‐Fukuhara, M., Angoulvant, A., & Lelandais, G. (2020) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqaa027 · Cited by 11 · see citing works
Zheng, D., Yue, D., Shen, J., Li, D., Song, Z., Huang, Y., Yong, J., & Li, Y. (2023) · Journal of Applied Microbiology · doi:10.1093/jambio/lxad276 · Cited by 10 · see citing works
Sahu, M. S., Purushotham, R., & Kaur, R. (2024) · PLoS Genetics · doi:10.1371/journal.pgen.1011281 · Cited by 6 · see citing works
Self-citationPhosphatidylinositol 3-phosphate regulates iron transport via PI3P-binding CgPil1 protein
Askari, F., Vasavi, B., & Kaur, R. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112855 · Cited by 4 · see citing works
Self-citationLipidomics Approaches: Applied to the Study of Pathogenesis in Candida Species
Singh, A., Khandelwal, N., & Prasad, R. (2019) · Progress in molecular and subcellular biology · doi:10.1007/978-3-030-13035-0_8 · Cited by 2 · see citing works
Meeting report – the Microtubules, Motors, Transport and Trafficking (M2T2) 2019 meeting
Ananthanarayanan, V., & Mylavarapu, S. V. S. (2020) · Journal of Cell Science · doi:10.1242/jcs.245928 · Cited by 1 · see citing works
Askari, F., & Kaur, R. (2023) · STAR Protocols · doi:10.1016/j.xpro.2023.102759
Self-citationTranscriptional networks of the stress responses in the human pathogen Candida glabrata
Thiébaut, A. (2018) · theses.fr (ABES) · doi:10.70675/323c74a8z1ae4z4123za081zd0af3ecf65ae
TPC1-dependent control of endosomal pH and transferrin uptake determines cellular iron status
Deutsch, R., Jörs, S., Klingl, Y. E., Kudrina, V., Menegaz, D., Jaślan, D., Serianz, Z., Vogel, A., Abrahamian, C., Bhunia, S., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2602941123
Gómez-Gaviria, M., Ramírez-Sotelo, U., & Mora-Montes, H. M. (2026) · Journal of Fungi · doi:10.3390/jof12100791
- Authors
- Sharma, V., Purushotham, R., & Kaur, R.
- Affiliations
- Manipal Academy of Higher Education (IN)
- Centre for DNA Fingerprinting and Diagnostics (IN)
- Corresponding author
- Kaur, Rupinder
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 291
- Issue
- 47
- Pages
- 24715-24734
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5114420
- OpenAlex
- W2531585364
- Cited by
- 22
- References
- 61
- Citations by year
- 2026: 2 · 2024: 1 · 2023: 5 · 2022: 1 · 2020: 6 · 2019: 4 · 2018: 1 · 2017: 2
- FWCI
- 1.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Department of Biotechnology, Ministry of Science and Technology (BT/PR5145/MED/29/470/2012, BT/PR7388/MED/29/650/2012, BT/PR7123/BRB/10/1149/2012)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
- Keywords
- phosphatidylinositol 3-kinase, Candida glabrata, iron homeostasis, iron permease, retrograde trafficking, vesicle trafficking, iron acquisition, iron limitation, iron overload, vacuoles, biofilm formation, macrophage survival, host colonization, phosphatidylinositol 3-phosphate
- MeSH terms
- Animals, Candidiasis, Female, Fungal Proteins, Iron, Macrophages, Mice, Inbred BALB C, Phosphatidylinositol 3-Kinases, Membrane Transport Proteins, Candida glabrata, Mice
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