The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Constitutive Activation of Chaperone-mediated Autophagy in Cells with Impaired Macroautophagy
Open accessAbstract
Three different types of autophagy—macroautophagy, microautophagy, and chaperone-mediated autophagy (CMA)—contribute to degradation of intracellular components in lysosomes in mammalian cells. Although some level of basal macroautophagy and CMA activities has been described in different cell types and tissues, these two pathways are maximally activated under stress conditions. Activation of these two pathways is often sequential, suggesting the existence of some level of cross-talk between both stress-related autophagic pathways. In this work, we analyze the consequences of blockage of macroautophagy on CMA activity. Using mouse embryonic fibroblasts deficient in Atg5, an autophagy-related protein required for autophagosome formation, we have found that blockage of macroautophagy leads to up-regulation of CMA, even under basal conditions. Interestingly, different mechanisms contribute to the observed changes in CMA-related proteins and the consequent activation of CMA during basal and stress conditions in these macroautophagy-deficient cells. This work supports a direct cross-talk between these two forms of autophagy, and it identifies changes in the lysosomal compartment that underlie the basis for the communication between both autophagic pathways.
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
Cites
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Self-citationLoss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Self-citationRavikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331
Self-citationReactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · cited 2×
“Macroautophagy and CMA activity are maximally activated under stress conditions such as starvation, oxidative stress, or conditions leading to enhanced protein misfolding (Cuervo et al., 1995; Kiffin et al., 2004; Mizushima et al., 2004; Ravikumar et al., 2004; Iwata et al., 2005; Scherz-Shouval et al., 2007).”
BackgroundImpaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · cited 3×
“…soluble forms of misfolded proteins, bearing the CMA-targeting motif, can be readily degraded via CMA; however, because the misfolded proteins organize in multimeric complexes, they block the CMA translocation machinery and they can no longer be degraded through this pathway (Cuervo et al., 2004).”
BackgroundSelf-citationThe role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
Nakai, A., Yamaguchi, O., Takeda, T., Higuchi, Y., Hikoso, S., Taniike, M., Omiya, S., Mizote, I., Matsumura, Y., Asahi, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1574 · Cited by 1,520
Self-citationLithium induces autophagy by inhibiting inositol monophosphatase
Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985
Cited by
The coming of age of chaperone-mediated autophagy
Kaushik, S., & Cuervo, A. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0001-6 · Cited by 1,407
Self-citationDegradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898
Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899
Self-citationAutophagy gone awry in neurodegenerative diseases
Wong, E., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 815
Self-citationZhang, C., & Cuervo, A. M. (2008) · Nature Medicine · doi:10.1038/nm.1851 · Cited by 520
Self-citationReduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson’s disease
Murphy, K. E., Gysbers, A. M., Abbott, S. K., Tayebi, N., Kim, W. S., Sidransky, E., Cooper, A., Garner, B., & Halliday, G. M. (2014) · Brain · doi:10.1093/brain/awt367 · Cited by 475
Gómez-Virgilio, L., Silva-Lucero, M.-D.-C., Flores-Morelos, D.-S., Gallardo-Nieto, J., Lopez-Toledo, G., Abarca-Fernandez, A.-M., Zacapala-Gómez, A.-E., Luna-Muñoz, J., Montiel-Sosa, F., Soto-Rojas, L. O., et al. (2022) · Cells · doi:10.3390/cells11152262 · Cited by 431
Ramos, F. J., Chen, S. C., Garelick, M. G., Dai, D.-F., Liao, C.-Y., Schreiber, K. H., MacKay, V. L., An, E. H., Strong, R., Ladiges, W. C., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003802 · Cited by 349
ROS-induced autophagy in cancer cells assists in evasion from determinants of immunogenic cell death
Garg, A. D., Dudek, A. M., Ferreira, G. B., Verfaillie, T., Vandenabeele, P., Krysko, D. V., Mathieu, C., & Agostinis, P. (2013) · Autophagy · doi:10.4161/auto.25399 · Cited by 305
Autophagy and the hallmarks of aging
Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285
Self-citationRegulation of the aging process by autophagy.
Salminen, A., & Kaarniranta, K. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.03.004 · Cited by 270
Chaperone-mediated autophagy: selectivity pays off
Cuervo, A. M. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.10.003 · Cited by 260
“For example, RNA interference against LAMP-2A, which blocks CMA results in constitutive activation of macroautophagy and vice versa; however, both pathways are non-redundant, and the lack of the defective pathway becomes evident in response to an additional stressor [25,27].”
BackgroundSelf-citationChaperone-mediated autophagy. Molecular mechanisms and physiological relevance
Orenstein, S. J., & Cuervo, A. M. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.02.005 · Cited by 260
Self-citationUbiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
Rothenberg, C., Srinivasan, D., Mah, L., Kaushik, S., Peterhoff, C. M., Ugolino, J., Fang, S., Cuervo, A. M., Nixon, R. A., & Monteiro, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq231 · Cited by 225
Self-citationPajares, M., Rojo, A. I., Arias, E., Díaz-Carretero, A., Cuervo, A. M., & Cuadrado, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1474992 · Cited by 218
Self-citationAutophagy 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
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189
“Granulophagy can also serve a compensatory role in the setting of dysfunctional macroautophagy [67].”
BackgroundAutophagy in disease: a double-edged sword with therapeutic potential
Martinet, W., Agostinis, P., Vanhoecke, B., Dewaele, M., & de Meyer, G. R. Y. (2009) · Clinical Science · doi:10.1042/cs20080508 · Cited by 186
LAMP2A, LAMP2B and LAMP2C: similar structures, divergent roles
Qiao, L., Hu, J., Qiu, X., Wang, C., Peng, J., Zhang, C., Zhang, M., Lu, H., & Chen, W. (2023) · Autophagy · doi:10.1080/15548627.2023.2235196 · Cited by 174
Chaperone-mediated autophagy. Machinery, regulation and biological consequences
Li, W., Yang, Q., & Mao, Z. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0565-6 · Cited by 119
Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases
Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111
Chen, X., Li, Y., Wang, C., Tang, Y., Mok, S.-A., Tsai, R. M., Rojas, J. C., Karydas, A., Miller, B. L., Boxer, A. L., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0354-0 · Cited by 107
Self-citationTargeting the Autophagy/Lysosomal Degradation Pathway in Parkinsons Disease
Rivero-Ríos, P., Madero-Pérez, Fernández, B., & Hilfiker, S. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666151030103027 · Cited by 69
Comprehensive autophagy evaluation in cardiac disease models
Kaludercic, N., Maiuri, M. C., Kaushik, S., Fernández, Á. F., de Bruijn, J., Castoldi, F., Chen, Y., Ito, J., Mukai, R., Murakawa, T., et al. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvz233 · Cited by 64
Self-citationAutophagy in Alzheimer’s disease
Moreira, P. I., Santos, R. X., Zhu, X., Lee, H.-G., Smith, M. A., Casadesus, G., & Perry, G. (2010) · Expert Review of Neurotherapeutics · doi:10.1586/ern.10.84 · Cited by 55
Chaperone-Mediated Autophagy and Its Emerging Role in Hematological Malignancies
Robert, G., Jacquel, A., & Auberger, P. (2019) · Cells · doi:10.3390/cells8101260 · Cited by 45
Wang, M., & Miller, R. A. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00833.x · Cited by 45
Fote, G. M., Geller, N. R., Efstathiou, N. E., Hendricks, N., Vavvas, D. G., Reidling, J. C., Thompson, L. M., & Steffan, J. S. (2022) · Journal of Cell Science · doi:10.1242/jcs.258687 · Cited by 36
Perusek, L., Sahu, B., Parmar, T., Maeno, H., Arai, E., Le, Y.-Z., Subauste, C. S., Chen, Y., Palczewski, K., & Maeda, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.682310 · Cited by 35
Chauhan, A. S., Kumar, M., Chaudhary, S., Dhiman, A., Patidar, A., Jakhar, P., Jaswal, P., Sharma, K., Sheokand, N., Malhotra, H., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201802102r · Cited by 29
The fine-tuning of proteolytic pathways in Alzheimer’s disease
Cecarini, V., Bonfili, L., Cuccioloni, M., Mozzicafreddo, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2238-6 · Cited by 21
(2012) · PubMed
Metadata
- Authors
- Kaushik, S., Massey, A. C., Mizushima, N., & Cuervo, A. M.
- Venue
- Molecular Biology of the Cell
- Published
- 2008-05
- Volume
- 19
- Issue
- 5
- Pages
- 2179-2192
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2101962395
- Cited by
- 335
- References
- 11
- FWCI
- 12.26
- 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.
