The DOI matches its Crossref record.
Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction.
Open accessAbstract
For determination of the physiological role and mechanism of vacuolar proteolysis in the yeast Saccharomyces cerevisiae, mutant cells lacking proteinase A, B, and carboxypeptidase Y were transferred from a nutrient medium to a synthetic medium devoid of various nutrients and morphological changes of their vacuoles were investigated. After incubation for 1 h in nutrient-deficient media, a few spherical bodies appeared in the vacuoles and moved actively by Brownian movement. These bodies gradually increased in number and after 3 h they filled the vacuoles almost completely. During their accumulation, the volume of the vacuolar compartment also increased. Electron microscopic examination showed that these bodies were surrounded by a unit membrane which appeared thinner than any other intracellular membrane. The contents of the bodies were morphologically indistinguishable from the cytosol; these bodies contained cytoplasmic ribosomes, RER, mitochondria, lipid granules and glycogen granules, and the density of the cytoplasmic ribosomes in the bodies was almost the same as that of ribosomes in the cytosol. The diameter of the bodies ranged from 400 to 900 nm. Vacuoles that had accumulated these bodies were prepared by a modification of the method of Ohsumi and Anraku (Ohsumi, Y., and Y. Anraku. 1981. J. Biol. Chem. 256:2079-2082). The isolated vacuoles contained ribosomes and showed latent activity of the cytosolic enzyme glucose-6-phosphate dehydrogenase. These results suggest that these bodies sequestered the cytosol in the vacuoles. We named these spherical bodies "autophagic bodies." Accumulation of autophagic bodies in the vacuoles was induced not only by nitrogen starvation, but also by depletion of nutrients such as carbon and single amino acids that caused cessation of the cell cycle. Genetic analysis revealed that the accumulation of autophagic bodies in the vacuoles was the result of lack of the PRB1 product proteinase B, and disruption of the PRB1 gene confirmed this result. In the presence of PMSF, wild-type cells accumulated autophagic bodies in the vacuoles under nutrient-deficient conditions in the same manner as did multiple protease-deficient mutants or cells with a disrupted PRB1 gene. As the autophagic bodies disappeared rapidly after removal of PMSF from cultures of normal cells, they must be an intermediate in the normal autophagic process. This is the first report that nutrient-deficient conditions induce extensive autophagic degradation of cytosolic components in the vacuoles of yeast cells.
Overview
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
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Guidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996
Self-citationAn Overview of Autophagy: Morphology, Mechanism, and Regulation
Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521
Gutierrez, M. G., Master, S. S., Singh, S. B., Taylor, G. A., Colombo, M. I., & Deretic, V. (2004) · Cell · doi:10.1016/j.cell.2004.11.038 · Cited by 2,252
Rabinowitz, J. D., & White, E. (2010) · Science · doi:10.1126/science.1193497 · Cited by 1,982
The pathways of mitophagy for quality control and clearance of mitochondria
Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900
Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy
Nicklin, P., Bergman, P., Zhang, B., Triantafellow, E., Wang, H., Nyfeler, B., Yang, H., Hild, M., Kung, C., Wilson, C., et al. (2009) · Cell · doi:10.1016/j.cell.2008.11.044 · Cited by 1,798
Growth factor regulation of autophagy and cell survival in the absence of apoptosis
Lum, J. J., Bauer, D. E., Kong, M., Harris, M. H., Li, C., Lindsten, T., & Thompson, C. B. (2005) · Cell · doi:10.1016/j.cell.2004.11.046 · Cited by 1,487
Yamamoto, A., Tagawa, Y., Yoshimori, T., Moriyama, Y., Masaki, R., & Tashiro, Y. (1998) · Cell Structure and Function · doi:10.1247/csf.23.33 · Cited by 1,312
Molecular dissection of autophagy: two ubiquitin-like systems
Ohsumi, Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056522 · Cited by 1,240
Self-citationBoland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0800-08.2008 · Cited by 1,119
Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
Tanida, I., Minematsu-Ikeguchi, N., Ueno, T., & Kominami, E. (2005) · Autophagy · doi:10.4161/auto.1.2.1697 · Cited by 1,108
Formation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast
Kirisako, T., Baba, M., Ishihara, N., Miyazawa, K., Ohsumi, M., Yoshimori, T., Noda, T., & Ohsumi, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.435 · Cited by 881
“Subsequently, autophagic body is released into the vacuolar lumen (Takeshige et al., 1992; Baba et al., 1994).”
BackgroundSelf-citationMitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy
Okamoto, K., Kondo-Okamoto, N., & Ohsumi, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.013 · Cited by 797
Self-citationA brief history of autophagy from cell biology to physiology and disease
Mizushima, N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0092-5 · Cited by 696
Methods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656
Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
Mochida, K., Oikawa, Y., Kimura, Y., Kirisako, H., Hirano, H., Ohsumi, Y., & Nakatogawa, H. (2015) · Nature · doi:10.1038/nature14506 · Cited by 611
Self-citationYoshimoto, K., Hanaoka, H., Sato, S., Kato, T., Tabata, S., Noda, T., & Ohsumi, Y. (2004) · The Plant Cell · doi:10.1105/tpc.104.025395 · Cited by 603
Self-citationAutophagosome–lysosome fusion is independent of V-ATPase-mediated acidification
Mauvezin, C., Nagy, P., Juhász, G., & Neufeld, T. P. (2015) · Nature Communications · doi:10.1038/ncomms8007 · Cited by 424
Piecemeal Microautophagy of Nucleus in Saccharomyces cerevisiae
Roberts, P., Moshitch-Moshkovitz, S., Kvam, E., O'Toole, E., Winey, M., & Goldfarb, D. S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-08-0483 · Cited by 409
Diverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376
Autophagy and Alzheimer’s Disease: From Molecular Mechanisms to Therapeutic Implications
Uddin, M. S., Stachowiak, A., Mamun, A. A., Tzvetkov, N. T., Takeda, S., Atanasov, A. G., Bergantin, L. B., Abdel-Daim, M. M., & Stankiewicz, A. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00004 · Cited by 395
Mitophagy: An Emerging Role in Aging and Age-Associated Diseases
Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359
Cysteine Metabolism in Neuronal Redox Homeostasis
Paul, B. D., Sbodio, J. I., & Snyder, S. H. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.02.007 · Cited by 356
Mitophagy in Yeast Occurs through a Selective Mechanism
Kanki, T., & Klionsky, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802403200 · Cited by 335
Atg17 Functions in Cooperation with Atg1 and Atg13 in Yeast Autophagy
Kabeya, Y., Kamada, Y., Baba, M., Takikawa, H., Sasaki, M., & Ohsumi, Y. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0669 · Cited by 304
Self-citationTwo Distinct Pathways for Targeting Proteins from the Cytoplasm to the Vacuole/Lysosome
Baba, M., Osumi, M., Scott, S. V., Klionsky, D. J., & Ohsumi, Y. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1687 · Cited by 292
Self-citationApg10p, a novel protein‐conjugating enzyme essential for autophagy in yeast
Shintani, T., Mizushima, N., Ogawa, Y., Matsuura, A., Noda, T., & Ohsumi, Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5234 · Cited by 269
Self-citationTal, R., Winter, G., Ecker, N., Klionsky, D. J., & Abeliovich, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m605940200 · Cited by 268
Cheong, H., Nair, U., Geng, J., & Klionsky, D. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-08-0826 · Cited by 245
Kuma, A., & Mizushima, N. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.002 · Cited by 237
Scott, S. V., Nice, D. C., Nau, J. J., Weisman, L. S., Kamada, Y., Keizer-Gunnink, I., Funakoshi, T., Veenhuis, M., Ohsumi, Y., & Klionsky, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002813200 · Cited by 227
Self-citationDivergent modes of autophagy in the methylotrophic yeast Pichia pastoris
Tuttle, D. L., & Dunn, W. A. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.1.25 · Cited by 206
Guan, J., Stromhaug, P. E., George, M. D., Habibzadegah-Tari, P., Bevan, A., Dunn, W. A., & Klionsky, D. J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.12.3821 · Cited by 204
Autophagy and Its Normal and Pathogenic States in the Brain
Yamamoto, A., & Yue, Z. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014149 · Cited by 204
Inoue, Y., Suzuki, T., Hattori, M., Yoshimoto, K., Ohsumi, Y., & Moriyasu, Y. (2006) · Plant and Cell Physiology · doi:10.1093/pcp/pcl031 · Cited by 189
Self-citationAtg17 Regulates the Magnitude of the Autophagic Response
Cheong, H., Yorimitsu, T., Reggiori, F., Legakis, J. E., Wang, C.-W., & Klionsky, D. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-10-0894 · Cited by 187
Analysis of the Membrane Structures Involved in Autophagy in Yeast by Freeze-Replica Method.
Baba, M., Osumi, M., & Ohsumi, Y. (1995) · Cell Structure and Function · doi:10.1247/csf.20.465 · Cited by 151
Self-citationAutophagy in animal development
Allen, E. A., & Baehrecke, E. H. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-020-0497-0 · Cited by 127
Cysteine peptidases CPA and CPB are vital for autophagy and differentiation in Leishmania mexicana
Williams, R. A., Tetley, L., Mottram, J. C., & Coombs, G. H. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05274.x · Cited by 140
Abeliovich, H., Darsow, T., & Emr, S. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6005 · Cited by 126
Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p
Barth, H., Meiling-Wesse, K., Epple, U. D., & Thumm, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03016-2 · Cited by 123
The coordinated action of the MVB pathway and autophagy ensures cell survival during starvation
Müller, M., Schmidt, O., Angelova, M., Faserl, K., Weys, S., Kremser, L., Pfaffenwimmer, T., Dalik, T., Kraft, C., Trajanoski, Z., et al. (2015) · eLife · doi:10.7554/elife.07736 · Cited by 117
Abeliovich, H., Zarei, M., Rigbolt, K. T. G., Youle, R. J., & Dengjel, J. (2013) · Nature Communications · doi:10.1038/ncomms3789 · Cited by 114
Identification of Novel Vesicles in the Cytosol to Vacuole Protein Degradation Pathway
Huang, P.-H., & Chiang, H.-L. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.4.803 · Cited by 98
Enhancing autophagy in Alzheimer's disease through drug repositioning
Eshraghi, M., Ahmadi, M., Afshar, S., Lorzadeh, S., Adlimoghaddam, A., Rezvani Jalal, N., West, R., Dastghaib, S., Igder, S., Torshizi, S. R. N., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108171 · Cited by 89
Petroi, D., Popova, B., Taheri-Talesh, N., Irniger, S., Shahpasandzadeh, H., Zweckstetter, M., Outeiro, T. F., & Braus, G. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361865 · Cited by 81
Quantification of nonselective bulk autophagy in S. cerevisiae using Pgk1-GFP
Welter, E., Thumm, M., & Krick, R. (2010) · Autophagy · doi:10.4161/auto.6.6.12348 · Cited by 69
Cell deaths: Involvement in the pathogenesis and intervention therapy of COVID-19
Li, X., Zhang, Z., Wang, Z., Gutiérrez-Castrellón, P., & Shi, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01043-6 · Cited by 67
Autophagic cell death: Analysis in Dictyostelium
Giusti, C., Tresse, E., Luciani, M.-F., & Golstein, P. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.005 · Cited by 61
Regulation of mRNA Translation as a Conserved Mechanism of Longevity Control
Mehta, R., Chandler-Brown, D., Ramos, F. J., Shamieh, L. S., & Kaeberlein, M. (2010) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4419-7002-2_2 · Cited by 44
Peck Justice, S. A., Barron, M. P., Qi, G. D., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Vilseck, J. Z., Wijeratne, A. B., & Mosley, A. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014576 · Cited by 28
Peck Justice, S. A., Qi, G., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Wijeratne, A. B., & Mosley, A. L. (2019) · doi:10.1101/2019.12.30.891267 · Cited by 28
Atg15 is a vacuolar phospholipase that disintegrates organelle membranes
Watanabe, Y., Iwasaki, Y., Sasaki, K., Motono, C., Imai, K., & Suzuki, K. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113567 · Cited by 17
Reappraisal of Antimalarials in Interferonopathies: New Perspectives for Old Drugs
Piscianz, E., Cuzzoni, E., Sharma, R., Tesser, A., Sapra, P., & Tommasini, A. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867324666170911162331 · Cited by 15
Minami, A., Nishi, K., Yamada, R., Jinnai, G., Shima, H., Oishi, S., Akagawa, H., Aono, T., Hidaka, M., Masaki, H., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108554 · Cited by 4
Metadata
- Authors
- Takeshige, K., Baba, M., Tsuboi, S., Noda, T., & Ohsumi, Y.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1992-10-15
- Volume
- 119
- Issue
- 2
- Pages
- 301-311
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2126801593
- Cited by
- 1,264
- References
- 0
- FWCI
- 9.06
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
