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Chaperone-mediated autophagy: selectivity pays off
Open accessAbstract
Degradation of intracellular components in lysosomes, generically known as autophagy, can occur through different pathways. This review discusses chaperone-mediated autophagy (CMA), a type of autophagy set apart from other autophagic pathways owing to its selectivity and distinctive mechanism by which substrates reach the lysosomal lumen. CMA participates in quality control and provides energy to cells under persistently poor nutritional conditions. Alterations in CMA have recently been shown to underlie some severe human disorders for which the decline with age in the activity of this pathway might become a major aggravating factor. Prevention of the age-dependent decline in CMA has major beneficial effects on cellular and organ homeostasis and function, revealing that CMA is an essential component of the anti-aging fight.
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“Three different forms of autophagy have been described in mammalian cells: macroautophagy, microautophagy and chaperone-mediated autophagy (Fig. 3) (Cuervo, 2009; He and Klionsky, 2009; Mizushima et al., 2008).”
From Protein Homeostasis and Aging: the importance of exquisite quality control (2011) · cites this paper as Cuervo, 2009
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Citations
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Self-citationIntegration of Clearance Mechanisms: The Proteasome and AutophagyPreprint
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“CMA is a highly selective form of autophagy that requires unfolding of the protein before internalization into the lysosome for degradation (Dice, 2007; Cuervo, 2010).”
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Klionsky, D. J., Baehrecke, E. H., Brumell, J. H., Chu, C. T., Codogno, P., Cuervo, A. M., Debnath, J., Deretic, V. P., Elazar, Z., Eskelinen, E., et al. (2011) · Autophagy · doi:10.4161/auto.7.11.17661 · Cited by 298
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“Interested readers are referred to more focused reviews [2,3,8,29,54] for a comprehensive description of the molecular apparatus executing these different autophagic pathways.”
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“Mutation-based impairment of chaperone proteins [9], as well as proteins involved with the ubiquitin proteasomal [10, 11] and the autophagy lysosomal [12, 13] systems, has been described.”
BackgroundUbiquilin 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
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Bandyopadhyay, U., Sridhar, S., Kaushik, S., Kiffin, R., & Cuervo, A. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.004 · Cited by 240
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InfluentialSelf-citationRegulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage
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Self-citationChaperone-mediated autophagy at a glance
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“Analyses of cellular conditions that activate CMA, substrates degraded under these conditions and the consequences of blocking this pathway in cultured cells have helped to understand the cellular functions of CMA (Dice, 2007; Cuervo, 2010).”
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Mehrpour, M., Esclatine, A., Beau, I., & Codogno, P. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00507.2009 · Cited by 211
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Loss of hepatic chaperone‐mediated autophagy accelerates proteostasis failure in aging
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“Introduction In chaperone-mediated autophagy (CMA) (Cuervo, 2010; Kaushik & Cuervo, 2012), cytosolic proteins bearing a targeting motif biochemically related to the pentapeptide KFERQ (Dice, 1990) are recognized by the chaperone hsc70 that delivers them one-by-one to lysosomes for degradation (Chiang et al.”
BackgroundSelf-citationHeat Shock Proteins: Cell Protection through Protein Triage
Lanneau, D., Wettstein, G., Bonniaud, P., & Garrido, C. (2010) · The Scientific World JOURNAL · doi:10.1100/tsw.2010.152 · Cited by 191
“HSC70, associated with cochaperones, participates in CMA by recognizing a motif related to the pentapeptide KFERQ and directing it to lysomal degradation[11].”
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A comprehensive glossary of autophagy-related molecules and processes
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“Chaperone-mediated autophagy (CMA): An autophagic process in mammalian cells by which proteins containing a particular pentapeptide motif related to KFERQ are transported across the lysosomal membrane and degraded.(72,73) The translocation process requires the action of the integral membrane protein LAMP-2A and both c…”
BackgroundSelf-citationMartínez-López, N., Athonvarangkul, D., & Singh, R. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-2404-2_3 · Cited by 185
“The binding of substrate to monomeric form of LAMP-2A is followed by substrate unfolding possibly assisted by hsc70 and its co-chaperones [10].”
BackgroundSTUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy
Ferreira, J. V., Fofo, H., Bejarano, E., Bento, C. F., Ramalho, J. S., Girão, H., & Pereira, P. (2013) · Autophagy · doi:10.4161/auto.25190 · Cited by 187
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“Upregulation of chaperonemediated autophagy (CMA), the other stress-induced autophagic pathway in mammals (Cuervo, 2010), has been previously described in vitro in macroautophagy-deficient cell lines (Kaushik et al.”
BackgroundInfluentialSelf-citationConstitutive Upregulation of Chaperone-Mediated Autophagy in Huntington's Disease
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“…to experimental blockage in macroautophagy by upregulating chaperone-mediated autophagy (CMA) (Kaushik et al., 2008), a type of autophagy conducive to degradation of cytosolic proteins in lysosomes through direct translocation across the membrane of these organelles (Dice, 2007; Cuervo, 2010).”
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“We next considered whether chaperone-mediated autophagy (CMA), an alternative degradation pathway by which client proteins are targeted by heat-shock protein Hsc70 and its co-chaperones for lysosomal destruction (Figure 6A)(Cuervo, 2010), could be involved.”
BackgroundAutophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1
Toledo, M., Batista‐González, A., Merheb, E., Aoun, M. L., Tarabra, E., Feng, D., Sarparanta, J., Merlo, P., Botrè, F., Schwartz, G. J., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.023 · Cited by 169
“Autophagy Degrades CRY1 in a Time-Dependent Manner Three distinct mechanisms deliver cargo to lysosomes: macroautophagy (or autophagy) (He and Klionsky, 2009), chaperonemediated autophagy (CMA) (Cuervo, 2010), and endosomal microautophagy (eMI) (Sahu et al.”
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“It is well known that blockage of macroautophagy can lead to a compensatory upregulation of CMA [26], an alternative lysosome-mediated degradation pathway wherein cytosolic components are directly translocated across the lysosomal membrane [36].”
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“The autophagosome fuses with the lysosome to create the autophagolysosome in which the luminal content is degraded [132-135].”
BackgroundAutophagy pathways activated in response to PDT contribute to cell resistance against ROS damage
Dewaele, M., Martinet, W., Rubio, N., Verfaillie, T., de Witte, P. A. M., Piette, J. G., & Agostinis, P. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01118.x · Cited by 139
“Journal of Cellular and Molecular Medicine © 2011 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd chaperone-substrate complex to the lysosomal-associated membrane protein 2 (LAMP2A), the receptor for CMA, followed by translocation of the unfolded substrate in the lysosomal lumen for degradation…”
BackgroundChaperone‐mediated autophagy in health and disease
Kon, M., & Cuervo, A. M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.025 · Cited by 141
“In contrast to micro- and macroautophagy, where whole regions of the cytosol are sequestered and delivered to lysosomes, CMA targets single cytosolic proteins to the lysosomal surface and mediates their one-by-one translocation across the lysosomal membrane for degradation [4,5].”
BackgroundInfluentialSelf-citationLAMP-2B regulates human cardiomyocyte function by mediating autophagosome–lysosome fusion
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“Chaperone-mediated autophagy (CMA) is a process of chaperondependent selection of cytosolic proteins that are translocated into the lysosome for degradation.”
BackgroundInfluentialHsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease
Salminen, A., Ojala, J. O., Kaarniranta, K., Hiltunen, M., & Soininen, H. S. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.006 · Cited by 131
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“Selectivity thus became one of the hallmarks of CMA [51].”
BackgroundDegradation of HK2 by chaperone-mediated autophagy promotes metabolic catastrophe and cell death
Xia, H.-G., Najafov, A., Geng, J., Galan-Acosta, L., Han, X., Guo, Y., Shan, B., Zhang, Y., Norberg, E., Zhang, T., et al. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201503044 · Cited by 122
“The CMA-targeting motif is degenerate and allows a series of amino acid combinations (Cuervo, 2010), and, consistently, an analysis with relaxed stringency revealed that almost 79% of all statistically decreased proteins had potential a CMA targeting motif, including p53 and Hsc70, which have been previously reported…”
Hu, X., Li, Z., Lin, R., Shan, J.-Q., Yu, Q., Wang, R., Liao, L., Yan, W., Zhen, W., Shang, L., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.634690 · Cited by 135
“…to the lumenal side of the lysosomal membrane by HSP90 Hsc70 with lysosomal markers (Immunofluorescence); LAMP2A (western blot); radiolabeling Cuervo, 2010; Parzych and Klionsky, 2014; Patel and Cuervo, 2015; Arias, 2017; Wu et al., 2019 Abbreviations: LAMP2A: lysosome-associated membrane…”
BackgroundNovel roles for α-crystallins in retinal function and disease
Kannan, R., Sreekumar, P. G., & Hinton, D. R. (2012) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2012.06.001 · Cited by 127
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“There is increasing evidence that members of the Hsp70 family may be directly implicated in protein degrading processes via shuttling their substrates to the degradation machinery, Cuervo has reported for example that Hsc70 is involved in chaperonemediated autophagy [15].”
BackgroundRole of Autophagy in Parkinson’s Disease
Cerri, S., & Blandini, F. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180226094351 · Cited by 107
Deneubourg, C., Ramm, M., Smith, L. J., Baron, O., Singh, K., Byrne, S., Duchen, M. R., Gautel, M., Eskelinen, E., Fanto, M., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1943177 · Cited by 115
“them into the lysosomes via LAMP2A (lysosomal associated membrane protein 2A) [9].”
BackgroundIntegrating the DNA damage and protein stress responses during cancer development and treatment
Gorgoulis, V. G., Pefani, D., Pateras, I. S., & Trougakos, I. P. (2018) · The Journal of Pathology · doi:10.1002/path.5097 · Cited by 108
“Its phosphorylation status determines whether the cell will bypass the “restriction point” of G1 phase committing the cell to progress to S phase without the requirements of extracellular stimulants [112-333].”
BackgroundModeling general proteostasis: proteome balance in health and disease
Roth, D., & Balch, W. E. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.11.001 · Cited by 113
“Likewise, the lysosome not only handles internalized cargoes from the cell surface, but is also a crucial partner of the autophagosome pathway that engulfs a wide range of misfolded cytosolic proteins and dysfunctional organelles [29,33].”
Dysregulation of autophagy and mitochondrial function in Parkinson’s disease
Wang, B., Abraham, N. A., Gao, G., & Yang, Q. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0065-1 · Cited by 112
“Notably, this motif is a pattern recognition motif associated with the hydrophobicity and charge of amino acid residues, rather than 100 % compliance with specific amino acid residues [26].”
BackgroundChaperone-mediated autophagy regulates proliferation by targeting RND3 in gastric cancer
Zhou, J., Yang, J., Fan, X., Hu, S., Zhou, F., Dong, J., Zhang, S., Shang, Y., Jiang, X., Guo, H., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1136770 · Cited by 104
“Macroautophagy and chaperone-mediated autophagy (CMA) are 2 well-characterized autophagic pathways in mammalian cells.(4,5) CMA is a selective process mediated in particular by HSPA8 and LAMP2A; HSPA8 can recognize and interact”
BackgroundRegulation of protein turnover by heat shock proteins
Bozaykut, P., Özer, N. K., & Karademir-Yilmaz, B. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.08.012 · Cited by 105
Viral Mediated Redirection of NEMO/IKKγ to Autophagosomes Curtails the Inflammatory Cascade
Fliss, P. M., Jowers, T. P., Brinkmann, M. M., Holstermann, B., Mack, C., Dickinson, P., Hohenberg, H., Ghazal, P., & Brune, W. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002517 · Cited by 111
“are bound by an Hsc70-containing chaperone complex and translocated directly into lysosomes without involvement of autophagosomes [55].”
BackgroundAge-Related Oxidative Stress Compromises Endosomal Proteostasis
Cannizzo, E. S., Clement, C. C., Morozova, K., Valdor, R., Kaushik, S., Almeida, L. N., Follo, C., Sahu, R., Cuervo, A. M., Macian, F., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.06.005 · Cited by 95
“…degree of oxidation still allows for the protein to be unfolded, which is a requirement for entry into the narrow catalytic chamber of the proteasome or the translocation channel that mediates substrate internalization into lysosomes via CMA (Dunlop et al., 2009; Cuervo, 2010; David et al., 2010).”
InfluentialSelf-citationChaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration
Koga, H., & Cuervo, A. M. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.07.006 · Cited by 98
Self-citationAutophagy, nutrition and immunology
Cuervo, A. M., & Macián, F. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.09.001 · Cited by 98
“In fact, failure to perform this cellular surveillance as a result of impaired autophagic function seems to underlie the basis of common protein conformational disorders, including severe neurodegenerative disorders and myopathies (Wong and Cuervo 2010).”
BackgroundSelf-citationAutophagic pathways and metabolic stress
Kaushik, S., Singh, R., & Cuervo, A. M. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01263.x · Cited by 95
“Activation of CMA during other types of stress also mediates the elimination of proteins damaged by the stressor [2].”
BackgroundInfluentialSelf-citationRout, A. K., Strub, M., Piszczek, G., & Tjandra, N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.609446 · Cited by 102
“It can target degradation of selective cytosolic proteins (36, 37).”
BackgroundZhang, J., Johnson, J. L., He, J. N., Napolitano, G., Ramadass, M., Rocca, C. J., Kiosses, W. B., Bucci, C., Xin, Q., Gavathiotis, E., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.764076 · Cited by 88
Self-citationSelective autophagy in the maintenance of cellular homeostasis in aging organisms
Hubbard, V. M., Valdor, R., Macián, F., & Cuervo, A. M. (2011) · Biogerontology · doi:10.1007/s10522-011-9331-x · Cited by 90
“Chaperone-mediated autophagy is responsible for the degradation of single soluble cytosolic proteins that are recognized by affinity binding of a chaperone to a pentapeptide motif in their sequence ( Cuervo 2010a; Kon and Cuervo 2010; Orenstein and Cuervo 2010).”
BackgroundInfluentialSelf-citationLinton, P., & Thoman, M. L. (2014) · Immunology Letters · doi:10.1016/j.imlet.2014.06.017 · Cited by 87
Autophagy in Toxicology: Cause or Consequence?
Orrenius, S., Kaminskyy, V. O., & Zhivotovsky, B. (2012) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140210 · Cited by 81
Rothaug, M., Stroobants, S., Schweizer, M., Peters, J., Zunke, F., Allerding, M., D’Hooge, R., Säftig, P., & Blanz, J. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0182-y · Cited by 82
“proteins in the lysosome via chaperone-mediated autophagy (CMA) [14,15] through recognition of a CMAtargeting motif, a pentapeptide sequence biochemically related to KFERQ present within 25–30% of all cytosolic proteins [16].”
BackgroundIntake of ω-6 Polyunsaturated Fatty Acid-Rich Vegetable Oils and Risk of Lifestyle Diseases
Yamashima, T., Ota, T., Mizukoshi, E., Nakamura, H., Yamamoto, Y., Kikuchi, M., Yamashita, T., & Kaneko, S. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa072 · Cited by 78
Chaperone-mediated autophagy: Dice's 'wild' idea about lysosomal selectivity
Cuervo, A. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3150 · Cited by 94
“The now-established details of the pathway can be found in recent review”
BackgroundSelf-citationChaperone-mediated autophagy prevents apoptosis by degrading BBC3/PUMA
Xie, W. D., Zhang, L., Jiao, H., Guan, L., Zha, J., Li, X., Wu, M., Wang, Z., Han, J., & You, H. (2015) · Autophagy · doi:10.1080/15548627.2015.1075688 · Cited by 82
Influence of Normal Aging on Brain Autophagy: A Complex Scenario
Loeffler, D. A. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00049 · Cited by 79
“Chaperone-mediated autophagy (Figure 2), a more selective autophagic mechanism than macroautophagy which has been identified only in mammals, does not involve vesicle formation (Cuervo, 2010).”
BackgroundInfluentialPark, H.-J., Shin, J. Y., Kim, H., Oh, S. H., & Lee, P. H. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.028 · Cited by 73
“Like the proteasome system, autophagy is a vital pathway for the refolding or removal of abnormal and aggregated proteins, and thus, acts as a cytoprotective response, particularly under stress or injury conditions (Cuervo, 2010; Levine and Kroemer, 2008; Mizushima et al., 2008; Rubinsztein, 2006).”
BackgroundSwovick, K., Firsanov, D., Welle, K. A., Hryhorenko, J. R., Wise, J. P., George, C., Sformo, T. L., Seluanov, A., Gorbunova, V., & Ghaemmaghami, S. (2021) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.002301 · Cited by 73
Han, Q., Deng, Y., Chen, S., Chen, R., Yang, M., Zhang, Z., Sun, X., Wang, W., He, Y., Wang, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04994-x · Cited by 73
Defective Autophagy in Parkinson’s Disease: Lessons from Genetics
Zhang, H., Duan, C., & Yang, H. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8787-5 · Cited by 72
“RNA interference of Lamp2a reduced CMA activity and decreased Lamp2a in dopaminergic cell lines, prolonging the half-life of α-synuclein [31, 32].”
BackgroundParkinson's disease: acid‐glucocerebrosidase activity and alpha‐synuclein clearance
Blanz, J., & Säftig, P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13517 · Cited by 75
Macroautophagy and Chaperone‐Mediated Autophagy in Heart Failure: The Known and the Unknown
Ghosh, R., & Pattison, J. S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8602041 · Cited by 72
“The translocation complex comprised of LAMP2a and a luminal HSC70 within the lysosomes (lys-HSC70) forms an integral part of the CMA machinery [81, 82].”
BackgroundGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, J., Abeliovich, H., Acevedo‐Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.5167/uzh-131237 · Cited by 69
Autophagic flux control in neurodegeneration: Progress and precision targeting—Where do we stand?
Lumkwana, D., du Toit, A., Kinnear, C. J., & Loos, B. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.006 · Cited by 69
“…directly into the lysosome through invagination of the lysosomal membrane (Cai et al., 2012 Nixon and Yang, 2011), while CMA involves a selective translocation of cytoplasmic proteins containing a KFERQ peptide motif into the lysosomal lumen (Cuervo, 2010; Dice, 2007; Klionsky et al., 2010).”
Hu, C., Zhao, L., Wu, D., & Li, L. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1225-x · Cited by 70
“Finally, CMA is a uniquely selective form of autophagy that degrades a wide range of substrate proteins after transporting them one by one into the lysosome [51].”
BackgroundAutophagy Modulation for Alzheimer’s Disease Therapy
Zhu, X., Yu, J., Jiang, T., & Tan, L. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8457-z · Cited by 66
Modulation of autophagy as new approach in mesenchymal stem cell-based therapy
Jakovljevic, J., Harrell, C. R., Fellabaum, C., Arsenijević, A., Jovicic, N. U., & Volarević, V. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.05.061 · Cited by 69
“CMA degrades a wide range of substrate proteins, including certain glycolytic enzymes, transcription factors and their inhibitors, calcium and lipid binding proteins, proteasome subunits, and proteins involved in vesicular trafficking [31].”
BackgroundCalpains and cancer: Friends or enemies?
Moretti, D., Bello, B. D., Allavena, G., & Maellaro, E. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.09.018 · Cited by 68
Chaperone mediated autophagy in aging: Starve to prosper
Xilouri, M., & Stefanis, L. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.001 · Cited by 65
Apelin/APJ system: A novel promising target for neurodegenerative diseases
Luo, H., Han, L., & Xu, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29001 · Cited by 61
“It is apparent that autophagic degradation is a preferential pathway for degradation of protein in the disease state due to progressive proteasomal impairment (Kaushik, Singh, & Cuervo, 2010).”
BackgroundZhang, L., Sun, Y., Fei, M., Tan, C., Wu, J., Zheng, J., Tang, J., Sun, W., Lv, Z., Bao, J., et al. (2014) · Autophagy · doi:10.4161/auto.28477 · Cited by 61
“In 2 of these mechanisms, macroautophagy and microautophagy, the substrates are engulfed or sequestered in bulk, whereas in CMA, the substrates are selectively transported across the lysosomal membrane on a one-by-one basis.(19) During CMA, protein substrates containing peptide regions similar to Lys-Phe-Glu-Arg-Gln (…”
BackgroundResultCan ‘calpain-cathepsin hypothesis’ explain Alzheimer neuronal death?
Yamashima, T. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.008 · Cited by 60
Zheng, Z., Zhang, L., Qu, Y., Xiao, G., Li, S., Bao, S., Lü, Q., & Mu, D. (2018) · Stem Cells · doi:10.1002/stem.2808 · Cited by 61
Bonhoure, A., Vallentin, A., Martin, M., Senff‐Ribeiro, A., Amson, R. B., Telerman, A., & Vidal, M. (2017) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.12.002 · Cited by 60
Induction of autophagy in temozolomide treated malignant gliomas
Natsumeda, M., Aoki, H., Miyahara, H., Yajima, N., Uzuka, T., Toyoshima, Y., Kakita, A., Takahashi, H., & Fujii, Y. (2011) · Neuropathology · doi:10.1111/j.1440-1789.2010.01197.x · Cited by 60
“In macroautophagy, large regions of the cytosol are sequestered, and is widely seen in eukaryocytes.(1,3,4,6,13) Chaperonemediated autophagy is a process in which single, soluble proteins are selectively sequestered and delivered to lysosomes, and is only seen in mammals.”
BackgroundProteostasis of Huntingtin in Health and Disease
Koyuncu, S., Fatima, A., Gutiérrez-García, R., & Vı́lchez, D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071568 · Cited by 61
“Whereas autophagy and microautophagy can degrade organelles and proteins, CMA is essentially involved in protein degradation [123].”
BackgroundAutophagy: A Role in the Apoptosis, Survival, Inflammation, and Development of the Retina
Lin, W., & Xu, G. (2018) · Ophthalmic Research · doi:10.1159/000487486 · Cited by 58
Lipids in autophagy: Constituents, signaling molecules and cargo with relevance to disease
Knævelsrud, H., & Simonsen, A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.01.001 · Cited by 55
Metadata
- Authors
- Cuervo, A. M.
- Venue
- Trends in Endocrinology & Metabolism
- Publisher
- Elsevier BV
- Published
- 2010-03
- Volume
- 21
- Issue
- 3
- Pages
- 142-150
- ISSN
- 1043-2760 (ISSN-L)
- PMC
- PMC2831144
- OpenAlex
- W1964976537
- Cited by
- 260
- References
- 61
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 5 · 2023: 12 · 2022: 8 · 2021: 12 · 2020: 18 · 2019: 11 · 2018: 20 · 2017: 20 · 2016: 25 · 2015: 18 · 2014: 19 · 2013: 19 · 2012: 16
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (R01AG021904, R37AG021904, P01AG031782, AG-021904, AG031782)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK041918, P01DK041918)
- National Institute of Neurological Disorders and Stroke (NS038370, P50NS038370)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- chaperone-mediated autophagy, lysosomal degradation, substrate specificity, quality control, energy homeostasis, nutritional stress, age-related decline, aging, age-related diseases, cellular homeostasis
- MeSH terms
- Animals, Autophagy, Humans, Lysosomes, Models, Biological, Molecular Chaperones
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