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The Sequential Activation of the Yeast HOG and SLT2 Pathways Is Required for Cell Survival to Cell Wall Stress
Open accessAbstract
Yeast mitogen-activated protein kinase (MAPK) signaling pathways transduce external stimuli into cellular responses very precisely. The MAPKs Slt2/Mpk1 and Hog1 regulate transcriptional responses of adaptation to cell wall and osmotic stresses, respectively. Unexpectedly, we observe that the activation of a cell wall integrity (CWI) response to the cell wall damage caused by zymolyase (β-1,3 glucanase) requires both the HOG and SLT2 pathways. Zymolyase activates both MAPKs and Slt2 activation depends on the Sho1 branch of the HOG pathway under these conditions. Moreover, adaptation to zymolyase requires essential components of the CWI pathway, namely the redundant MAPKKs Mkk1/Mkk2, the MAPKKK Bck1, and Pkc1, but it does not require upstream elements, including the sensors and the guanine nucleotide exchange factors of this pathway. In addition, the transcriptional activation of genes involved in adaptation to cell wall stress, like CRH1, depends on the transcriptional factor Rlm1 regulated by Slt2, but not on the transcription factors regulated by Hog1. Consistent with these findings, both MAPK pathways are essential for cell survival under these circumstances because mutant strains deficient in different components of both pathways are hypersensitive to zymolyase. Thus, a sequential activation of two MAPK pathways is required for cellular adaptation to cell wall damage.
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“Protein kinase C (PKC), high osmolarity glycerol response (HOG), and Ca+2-calcineurin pathways have been implicated in the response to cell wall damage and chitin synthesis (Figure 1B; Lagorce et al., 2003; Bermejo et al., 2008; Walker et al., 2008; Fortwendel et al., 2009).”
From Fungal Cell Wall: Emerging Antifungals and Drug Resistance. (2019) · cites this paper as Bermejo et al., 2008
Citations
Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860
Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,430
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
Methods in yeast genetics : a Cold Spring Harbor Laboratory course manual
Amberg, D. C., Burke, D. J., & Strathern, J. N. (2005) · Cited by 1,803
Osmotic Stress Signaling and Osmoadaptation in Yeasts
Hohmann, S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.2.300-372.2002 · Cited by 1,773
Cell Wall Integrity Signaling in Saccharomyces cerevisiae
Levin, D. E. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.2.262-291.2005 · Cited by 1,136
A two-component system that regulates an osmosensing MAP kinase cascade in yeast
Maeda, T., Wurgler‐Murphy, S. M., & Saito, H. (1994) · Nature · doi:10.1038/369242a0 · Cited by 1,072
Cell Wall Assembly in Saccharomyces cerevisiae
Lesage, G., & Bussey, H. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00038-05 · Cited by 849
Activation of Yeast PBS2 MAPKK by MAPKKKs or by Binding of an SH3-Containing Osmosensor
Maeda, T., Takekawa, M., & Saito, H. (1995) · Science · doi:10.1126/science.7624781 · Cited by 647
Fusion of Escherichia coli lacZ to the cytochrome c gene of Saccharomyces cerevisiae.
Guarente, L., & Ptashne, M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2199 · Cited by 528
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Alfatah, M., Bari, V. K., Nahar, A. S., Bijlani, S., & Ganesan, K. (2017) · Scientific Reports · doi:10.1038/srep40281 · Cited by 22
Signalling mechanisms involved in stress response to antifungal drugs
Víglaš, J., & Olejníková, P. (2020) · Research in Microbiology · doi:10.1016/j.resmic.2020.10.001 · Cited by 23
Zhao, Y., Li, S., Wang, J., Liu, Y., & Deng, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126169 · Cited by 22
Sellers-Moya, Á., Nuévalos, M., Molina, M., & Martı́n, H. (2021) · Journal of Fungi · doi:10.3390/jof7080647 · Cited by 21
Systems Level Analysis of the Yeast Osmo-Stat
Talemi, S. R., Tiger, C., Andersson, M., Babazadeh, R., Welkenhuysen, N., Klipp, E., Hohmann, S., & Schaber, J. (2016) · Scientific Reports · doi:10.1038/srep30950 · Cited by 22
Cadmium induces the activation of cell wall integrity pathway in budding yeast
Xiong, B., Zhang, L., Xu, H., Yang, Y., & Jiang, L. (2015) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2015.09.007 · Cited by 21
Li, X., Du, W., Zhao, J., Zhang, L., Zhu, Z., & Jiang, L. (2010) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2010.00626.x · Cited by 21
Jin, C., Kim, S. H., Willis, S. D., & Cooper, K. F. (2015) · Microbial Cell · doi:10.15698/mic2015.09.226 · Cited by 21
Response of Paracoccidioides brasiliensis Pb01 to stressor agents and cell wall osmoregulators
Tomazett, P. K., Castro, N. D. S., Lenzi, H. L., Soares, C. M. D. A., & Pereira, M. (2010) · Fungal Biology · doi:10.1016/j.funbio.2010.10.005 · Cited by 22
Gang, L., & Song, K. (2015) · FEBS Letters · doi:10.1002/1873-3468.12039 · Cited by 20
Kethireddy, V., Oey, I., Jowett, T. W. D., & Bremer, P. J. (2016) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2016.06.008 · Cited by 20
García, R., Itto‐Nakama, K., Rodríguez-Peña, J. M., Chen, X., Sanz, A. B., de Lorenzo, A., Pavón‐Vergés, M., Kubo, K., Ohnuki, S., Nombela, C., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202100278r · Cited by 20
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Nakic, Z. R., Seisenbacher, G., Posas, F., & Sauer, U. (2016) · BMC Systems Biology · doi:10.1186/s12918-016-0350-8 · Cited by 19
Self-citationSo, K.-K., Ko, Y., Chun, J., Kim, J., & Kim, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-09383-y · Cited by 19
Lam, M. H. Y., Snider, J. D., Rehal, M., Wong, V., Aboualizadeh, F., Drecun, L., Wong, O., Jubran, B., Li, M., Ali, M., et al. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.016 · Cited by 16
Ste11p MEKK signals through HOG, mating, calcineurin and PKC pathways to regulate the FKS2 gene
Wang, X., Sheff, M. A., Simpson, D. M., & Elion, E. A. (2011) · BMC Molecular Biology · doi:10.1186/1471-2199-12-51 · Cited by 16
Impact of Fungal MAPK Pathway Targets on the Cell Wall
Chow, J. L., Notaro, M. J., Prabhakar, A., Free, S. J., & Cullen, P. J. (2018) · Journal of Fungi · doi:10.3390/jof4030093 · Cited by 15
Rodríguez‐Escudero, I., Andrés‐Pons, A., Pulido, R., Molina, M., & Cid, V. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807867200 · Cited by 16
Negishi, T., Veis, J., Hollenstein, D. M., Sekiya, M., Ammerer, G., & Ohya, Y. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00952-15 · Cited by 17
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Laz, E. V., Lee, J., & Levin, D. E. (2019) · Fungal Biology · doi:10.1016/j.funbio.2019.10.002 · Cited by 16
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Berestovsky, N., Zhou, W., Nagrath, D., & Nakhleh, L. K. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003306 · Cited by 15
Steroid toxicity and detoxification in ascomycetous fungi
Cvelbar, D., Žist, V., Kobal, K., Žigon, D., & Žakelj‐Mavrič, M. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.11.025 · Cited by 15
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Escoté, X., Miranda, M., Rodríguez‐Porrata, B., Mas, A., Otero, R. R. C., Posas, F., & Vendrell, J. J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07585.x · Cited by 14
Self-citationBaranwal, S., Azad, G. K., Singh, V., & Tomar, R. S. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02393-13 · Cited by 16
Kim, H., Moon, H. Y., Lee, D.-J., Cheon, S. A., Yoo, S. J., Park, J., Agaphonov, M. O., Oh, D., Kwon, O., & Kang, H. A. (2013) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2013.08.003 · Cited by 14
Tanaka, Y., Sasaki, M., Ito, F., Aoyama, T., Okamoto, M., Takahashi‐Nakaguchi, A., Chibana, H., & Shibata, N. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161371 · Cited by 14
Fabri, J. H. T. M., Rocha, M. C., & Malavazi, I. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190705164203 · Cited by 13
Yeast Stress Response to Synthetic Constructs
Tartik, M. (2026) · ACS Synthetic Biology · doi:10.1021/acssynbio.5c00715 · Cited by 13
Venâncio, T. M., Balaji, S., Geetha, S., & Aravind, L. (2010) · Molecular BioSystems · doi:10.1039/c002567b · Cited by 13
García-Marqués, S., Rández‐Gil, F., & Prieto, J. A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.06.021 · Cited by 12
Miyamoto, M., Furuichi, Y., & Komiyama, T. (2012) · Yeast · doi:10.1002/yea.2927 · Cited by 12
Casagrande, V., Vescovo, V. D., Militti, C., Mangiapelo, E., Frontali, L., Negri, R., & Bianchi, M. M. (2009) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2009.00486.x · Cited by 12
KlHsl1 is a component of glycerol response pathways in the milk yeast Kluyveromyces lactis
Cialfi, S., Uccelletti, D., Carducci, A., Wésolowski‐Louvel, M., Mancini, P., Heipieper, H. J., & Saliola, M. (2011) · Microbiology · doi:10.1099/mic.0.044040-0 · Cited by 12
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Bereketoğlu, C., Arğa, K. Y., Eraslan, S., & Mertoğlu, B. (2017) · Physiological Genomics · doi:10.1152/physiolgenomics.00034.2017 · Cited by 12
Chen, H., Miller, P. W., Johnson, D. L., & Laribee, R. N. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009046 · Cited by 12
Yap4 PKA‐ and GSK3‐dependent phosphorylation affects its stability but not its nuclear localization
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Kim, H., Thak, E. J., Lee, D.-J., Agaphonov, M. O., & Kang, H. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129914 · Cited by 11
Kdx1 regulates RCK1 gene expression by interacting with Rlm1 in Saccharomyces cerevisiae
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Mesquita, I., Moreira, D., Sampaio‐Marques, B., Laforge, M., Cordeiro‐da‐Silva, A., Ludovico, P., Estaquier, J., & Silvestre, R. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_12 · Cited by 11
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Kim, H., Thak, E. J., Yeon, J. Y., Sohn, M. J., Choo, J. H., Kim, J., & Kang, H. A. (2018) · The Journal of Microbiology · doi:10.1007/s12275-018-7508-6 · Cited by 10
Dardalhon, M., Agoutin, B., Watzinger, M., & Averbeck, D. (2009) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2009.02.001 · Cited by 9
Lucas, C., Ferreira, C., Cazzanelli, G., Franco‐Duarte, R., & Tulha, J. (2016) · Journal of Developmental Biology · doi:10.3390/jdb4040033 · Cited by 10
Das, S., Goswami, A. M., & Saha, T. (2022) · Microbial Pathogenesis · doi:10.1016/j.micpath.2022.105418 · Cited by 9
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Suzuki, T., & Iwahashi, Y. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-012-0051-8 · Cited by 9
Jiang, L., Wang, L., Fang, T., & Papadopoulos, V. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.05.069 · Cited by 8
Bothammal, P., Prasad, M., Muralitharan, G., & Natarajaseenivasan, K. (2022) · Microbial Pathogenesis · doi:10.1016/j.micpath.2022.105840 · Cited by 8
Luo, G., Geng, Z., Kuerban, B., Xu, Y., Yang, J., Liu, J., & Li, M. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.998647 · Cited by 8
Lsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions
Veselá, P., Zahumenský, J., & Malinsky, J. (2023) · Journal of Cell Science · doi:10.1242/jcs.260554 · Cited by 8
Zheng, F., Gao, W., Wang, Y., Chen, Q., Zhang, Q., Jiang, X., Hou, B., & Zhang, Z. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12285 · Cited by 8
Eraso, P., Mazón, M. J., Posas, F., & Portillo, F. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07528.x · Cited by 7
Self-citationSharmin, D., Sasano, Y., Sugiyama, M., & Harashima, S. (2014) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2014.09.013 · Cited by 7
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Heinisch, J. J., & Rodicio, R. (2008) · Springer eBooks · doi:10.1007/978-3-540-85463-0_15 · Cited by 7
Queiroz, M. G., Elsztein, C., & de Morais, M. A. (2019) · Antonie van Leeuwenhoek · doi:10.1007/s10482-019-01335-y · Cited by 7
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Porras–Agüera, J. A., Mauricio, J. C., Moreno‐García, J., Moreno, J. J., & García‐Martínez, T. (2020) · Microorganisms · doi:10.3390/microorganisms8081188 · Cited by 6
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Wang, S., & Cheng, M. (2011) · Yeast · doi:10.1002/yea.1916 · Cited by 6
Tatjer, L., González, A., Serra‐Cardona, A., Barceló, A., Casamayor, A., & Ariño, J. (2016) · Molecular Microbiology · doi:10.1111/mmi.13416 · Cited by 6
Identifying Candida albicans Gene Networks Involved in Pathogenicity
Thomas, G. H., Bain, J. M., Budge, S., Brown, A. J. P., & Ames, R. M. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00375 · Cited by 6
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Okada, H., Kono, K., Neiman, A. M., & Ohya, Y. (2016) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top078659 · Cited by 6
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Jann, C., Johansson, A., Smith, J., Parts, L., & Steinmetz, L. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.26.267674 · Cited by 5
Dilmetz, B. A., Brar, G. S., Desire, C. T., Meneses, J., Klingler‐Hoffmann, M., Young, C., & Hoffmann, P. (2024) · Foods · doi:10.3390/foods13162593 · Cited by 6
Pulido, V., Rodríguez-Peña, J. M., Alonso, G., Sanz, A. B., Arroyo, J., & García, R. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168570 · Cited by 6
Self-citationYu, L.-Y., Wang, T., Wang, B., & Pan, L. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137413 · Cited by 5
Lage, P., Coelho, B. B., Mira, N. P., & Mendes‐Ferreira, A. (2023) · Fermentation · doi:10.3390/fermentation9020172 · Cited by 4
Narula, K., Sinha, A., Choudhary, P., Ghosh, S., Elagamey, E., Sharma, A., Sengupta, A., Chakraborty, N., & Chakraborty, S. (2024) · Plant Direct · doi:10.1002/pld3.572 · Cited by 3
Sanz, A. B., Díez-Muñiz, S., Moya, J., Petryk, Y., Nombela, C., Rodríguez-Peña, J. M., & Arroyo, J. (2022) · Journal of Fungi · doi:10.3390/jof8070718 · Cited by 4
Self-citationKeyse, S. M. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00097-8 · Cited by 3
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Separovich, R. J., Karakatsanis, N. M., Gao, K., Fuh, D., Hamey, J. J., & Wilkins, M. R. (2024) · FEBS Journal · doi:10.1111/febs.17062 · Cited by 2
Rabies: risk, prognosis and prevention.
Driver, C. (2014) · PubMed · Cited by 2
Molecular Machines Involved in Pexophagy
Nazarko, T. Y., & Farré, J. (2014) · Springer eBooks · doi:10.1007/978-3-7091-1788-0_22 · Cited by 2
Malavia, D., Leaves, I., Onime, J., O'Neill, P., Yan, K., Brown, A. J., & Gow, N. A. R. (2026) · The Cell Surface · doi:10.1016/j.tcsw.2026.100170 · Cited by 1
Haberkorn, C., Gettle, N., Elsen, J., Medina-Chávez, N. O., Sivigny, J., Baselga‐Cervera, B., Greig, D., Travisano, M., Saxer, G., & Stelkens, R. B. (2026) · Evolution · doi:10.1093/evolut/qpag108 · Cited by 1
Sahoo, R., Husain, A., & Elion, E. A. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00163-7 · Cited by 1
Stacy, C. L., Scholes, A. N., Stuecker, T. N., Hood, S. E., Crystal, C., Espana-Pena, M., Paré, A. C., & Lewis, J. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.28.696518 · Cited by 1
Determination of the molecular and physiological basis of citric acid tolerance in spoilage yeast
McGuire, L. I. (2009) · UPT. Syiah Kuala University Library (Syiah Kuala University)
Antifungal Activity of Cationic Conjugated Polyelectrolytes and Oligomers against Candida albicans
Ingersol, L. J. (2014) · UNM’s Digital Repository (University of New Mexico)
Clock-Controlled Genes in Neurospora crassa.
Bennett, L. D., Beremand, P. D., Thomas, T. L., & Bell‐Pedersen, D. (2012)
Signaling of Infectious Growth in Fusarium oxysporum
Pérez‐Nadales, E., & Pietro, A. D. (2011) · Topics in current genetics · doi:10.1007/978-3-642-22916-9_4
Functional characterization of cell wall damage response genes in Arabidopsis thaliana
Carraca, L. P. V. (2012) · Spiral (Imperial College London) · doi:10.25560/11644
Global Analysis of Kinase Interactions in Budding Yeast using Synthetic Dosage Lethality
Sharifpoor, S. (2012) · TSpace (University of Toronto)
Sariki, S. K., Kumawat, R., Singh, V., & Tomar, R. S. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/463703
(2009) · Yeast · doi:10.1002/yea.1618
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Oz, N., Su, H., Sari, V., Patnaik, P. K., Hameed, R., Song, J. H., Prosser, D. C., Labunskyy, V. M., Gladyshev, V. N., Hao, N., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.14.648769 · Cited by 1
Ge, X., Cui, Y., Zhang, Y., Li, J., Wang, P., Yan, Z., & Qi, X. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104789
Engineering ATP Import in Yeast Uncovers a Synthetic Route to Extend Cellular LifespanPreprint
Oz, N., Su, H., Sari, V., Patnaik, P. K., Hameed, R., Song, J. H., Prosser, D. C., Labunskyy, V. M., Gladyshev, V. N., Hao, N., et al. (2026) · eLife · doi:10.7554/elife.109761.1
Engineering ATP Import in Yeast Uncovers a Synthetic Route to Extend Cellular LifespanPreprint
Oz, N., Su, H., Sari, V., Patnaik, P. K., Hameed, R., Song, J. H., Prosser, D. C., Labunskyy, V. M., Gladyshev, V. N., Hao, N., et al. (2026) · eLife · doi:10.7554/elife.109761
Su, X., Gajri, A., & Torres, M. P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.13.718172
Pavón‐Vergés, M., García, R., Rodríguez-Peña, J. M., Sanz, A. F., & Arroyo, J. (2026) · The FASEB Journal · doi:10.1096/fj.202504656rr
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Metadata
- Authors
- Bermejo, C., Rodríguez, E., García, R., Rodríguez-Peña, J. M., Rodríguez de la Concepción, M. L., Rivas, C., Arias, P., Nombela, C., Posas, F., & Arroyo, J.
- Affiliations
- Universidad Complutense de Madrid (ES)
- *Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid (UCM), 28040 Madrid, Spain; and
- Cell Signalling Unit, Department de Ciènces Experimentals I de la Salut, Universitat Pompeu Fabra (UPF), Parc de Recerca Biomèdica de Barcelona (PRBB), E-08003 Barcelona, Spain
- Universitat Pompeu Fabra (ES)
- ORCID
- Venue
- Molecular Biology of the Cell
- Published
- 2008-03
- Volume
- 19
- Issue
- 3
- Pages
- 1113-1124
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2262984
- OpenAlex
- W2103491947
- Cited by
- 204
- References
- 60
- Citations by year
- 2026: 11 · 2025: 4 · 2024: 8 · 2023: 6 · 2022: 9 · 2021: 7 · 2020: 8 · 2019: 9 · 2018: 9 · 2017: 6 · 2016: 16 · 2015: 18 · 2014: 17 · 2013: 7 · 2012: 15
- FWCI
- 7.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Johns Hopkins University
- Ministerio de Economía y Competitividad
- Universitat de Lleida
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- HOG pathway, cell wall integrity, MAPK signaling, zymolyase, β-1,3-glucanase, cell wall stress, osmotic stress, Sho1, PKC1, Rlm1, Saccharomyces cerevisiae, stress adaptation, cell survival
- MeSH terms
- Adaptation, Physiological, Cell Wall, Enzyme Activation, Hydrolases, Mutation, Phosphorylation, Saccharomyces cerevisiae, Transcriptional Activation, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System, Saccharomyces cerevisiae Proteins, Microbial Viability
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.
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