The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective
Open accessAbstract
The autophagy-lysosomal pathway (ALP) is involved in the degradation of long-lived proteins. Deficits in the ALP result in protein aggregation, the generation of toxic protein species, and accumulation of dysfunctional organelles, which are hallmarks of Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), and prion disease. Decades of research have therefore focused on enhancing the ALP in neurodegenerative diseases. More recently, transcription factor EB (TFEB), a major regulator of autophagy and lysosomal biogenesis, has emerged as a leading factor in addressing disease pathology. We review the regulation of the ALP and TFEB and their impact on neurodegenerative diseases. We also offer our perspective on the complex role of autophagy and TFEB in disease pathogenesis and its therapeutic implications through the examination of prion disease.
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TFE3 or TFEB upregulation or activation through pharmacological inhibition of mTORC1 can trigger clearance of excess α-synuclein and halt the progression of neurotoxicity.
“TFE3 or TFEB upregulation or activation through pharmacological inhibition of mTORC1 can trigger clearance of excess α-synuclein and halt the progression of neurotoxicity17–22.”
From PDCD4 triggers α-synuclein accumulation and motor deficits via co-suppressing TFE3 and TFEB translation in a model of Parkinson’s disease (2024) · cites this paper as [20]
The Parkinson’s Disease section reports that TFEB overexpression or activation ameliorates α-synuclein pathology, and that rapamycin inhibits mTOR and reduces that pathology in vitro and in vivo. It does not establish the same effect for TFE3 or show that these interventions halt the progression of neurotoxicity. (LLM, conf=0.86)
Experimental — accuracy not yet measuredMolecular and histopathologic analyses of patient tissues demonstrate mislocalized or accumulated autophagy machinery, pathogenic mutations underlying familial neurodegenerative diseases disable known autophagy-related factors, and genetically ablating autophagy effectors produces neurodegeneration in cell and animal model systems, supporting a role for autophagy dysfunction in age-related neurode
“Molecular and histopathologic analyses of patient tissues demonstrate mislocalized or accumulated autophagy machinery, pathogenic mutations underlying familial neurodegenerative diseases disable known autophagy-related factors, and genetically ablating autophagy effectors produce neurodegeneration in cell and animal model systems [74–81], supporting a role for autophagy dysfunction in the devel”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [79]
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875 · see citing works
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941 · see citing works
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 · see citing works
Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy
Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536 · see citing works
Loss 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 · see citing works
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365 · see citing works
Self-citationThe Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
A Gene Network Regulating Lysosomal Biogenesis and Function
Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543 · see citing works
Self-citationSancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · see citing works
Ravikumar, 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 · see citing works
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310 · see citing works
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
A lysosome‐to‐nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,932 · see citing works
Self-citationTransmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Autophagosomes form at ER–mitochondria contact sites
Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,747 · see citing works
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730 · see citing works
Kinesin and Dynein Superfamily Proteins and the Mechanism of Organelle Transport
Hirokawa, N. (1998) · Science · doi:10.1126/science.279.5350.519 · Cited by 1,689 · see citing works
Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673 · see citing works
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588 · see citing works
Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation
Hailey, D. W., Rambold, A. S., Satpute‐Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott‐Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,419 · see citing works
Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB
Medina, D. L., Paola, S. D., Peluso, I., Armani, A., Stefani, D. D., Venditti, R., Montefusco, S., Rosato, A. S., Prezioso, C., Forrester, A. R., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3114 · Cited by 1,405 · see citing works
Self-citationMTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
Martina, J. A., Chen, Y., Guček, M., & Puertollano, R. (2012) · Autophagy · doi:10.4161/auto.19653 · Cited by 1,360 · see citing works
Roczniak-Ferguson, A., Petit, C. S. V., Froehlich, F., Qian, S., Ky, J., Angarola, B. L., Walther, T. C., & Ferguson, S. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002790 · Cited by 1,358 · see citing works
Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341 · see citing works
Self-citationItakura, E., Kishi‐Itakura, C., & Mizushima, N. (2012) · Cell · doi:10.1016/j.cell.2012.11.001 · Cited by 1,327 · see citing works
Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212 · see citing works
Rapamycin-Induced Insulin Resistance Is Mediated by mTORC2 Loss and Uncoupled from Longevity
Lamming, D. W., Ye, L., Katajisto, P., Goncalves, M. D., Saitoh, M., Stevens, D. M., Davis, J. G., Salmon, A. B., Richardson, A., Ahima, R. S., et al. (2012) · Science · doi:10.1126/science.1215135 · Cited by 1,199 · see citing works
Pickford, F., Masliah, E., Britschgi, M., Lucin, K. M., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33585 · Cited by 1,186 · see citing works
TFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop
Settembre, C., De Cegli, R., Mansueto, G., Saha, P. K., Vetrini, F., Visvikis, O., Huynh, T., Carissimo, A., Palmer, D., Jürgen Klisch, T., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2718 · Cited by 1,022 · see citing works
Self-citationCharacterization of the CLEAR network reveals an integrated control of cellular clearance pathways
Palmieri, M., Impey, S., Kang, H., di Ronza, A., Pelz, C., Sardiello, M., & Ballabio, A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr306 · Cited by 1,022 · see citing works
Self-citationRogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992 · see citing works
Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967 · see citing works
Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939 · see citing works
Ragulator Is a GEF for the Rag GTPases that Signal Amino Acid Levels to mTORC1
Bar-Peled, L., Schweitzer, L. D., Zoncu, R., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.07.032 · Cited by 918 · see citing works
Microautophagy of Cytosolic Proteins by Late Endosomes
Sahu, R., Kaushik, S., Clement, C. C., Cannizzo, E. S., Scharf, B., Follenzi, A., Potolicchio, I., Nieves, E., Cuervo, A. M., & Santambrogio, L. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.12.003 · Cited by 902 · see citing works
Plasma membrane contributes to the formation of pre-autophagosomal structures
Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., & Rubinsztein, D. C. (2010) · Nature Cell Biology · doi:10.1038/ncb2078 · Cited by 902 · see citing works
Amino acid signalling upstream of mTOR
Jewell, J. L., Russell, R. C., & Guan, K.-L. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3522 · Cited by 894 · see citing works
Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885 · see citing works
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851 · see citing works
Chaperone-mediated autophagy: a unique way to enter the lysosome world
Kaushik, S., & Cuervo, A. M. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.05.006 · Cited by 850 · see citing works
Pathogenic Lysosomal Depletion in Parkinson's Disease
Dehay, B., Bové, J., Rodríguez-Muela, N., Perier, C., Recasens, A., Boya, P., & Vila, M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1920-10.2010 · Cited by 825 · see citing works
α-Synuclein impairs macroautophagy: implications for Parkinson’s disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works
Transcriptional control of autophagy-lysosome function drives pancreatic cancer metabolism
Perera, R. M., Stoykova, S., Nicolay, B. N., Ross, K. N., Fitamant, J., Boukhali, M., Lengrand, J., Deshpande, V., Selig, M. K., Ferrone, C. R., et al. (2015) · Nature · doi:10.1038/nature14587 · Cited by 799 · see citing works
In Vitro Generation of Infectious Scrapie Prions
Castilla, J., Saá, P., Hetz, C. A., & Soto, C. A. (2005) · Cell · doi:10.1016/j.cell.2005.02.011 · Cited by 790 · see citing works
Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N. R., Doi, H., Kurosawa, M., Nekooki, M., & Nukina, N. (2004) · Nature Medicine · doi:10.1038/nm985 · Cited by 777 · see citing works
TFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity
Decressac, M., Mattsson, B., Weikop, P., Lundblad, M., Jakobsson, J., & Björklund, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305623110 · Cited by 753 · see citing works
FoxO transcription factors; Regulation by AKT and 14-3-3 proteins
Tzivion, G., Dobson, M., & Ramakrishnan, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.002 · Cited by 728 · see citing works
Transcriptional Activation of Lysosomal Exocytosis Promotes Cellular Clearance
Medina, D. L., Fraldi, A., Bouchè, V., Annunziata, F., Mansueto, G., Spampanato, C., Puri, C., Pignata, A., Martina, J. A., Sardiello, M., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.07.016 · Cited by 708 · see citing works
Self-citationMartina, J. A., Diab, H. I., Lishu, L., Jeong-A, L., Patange, S., Raben, N., & Puertollano, R. (2014) · Science Signaling · doi:10.1126/scisignal.2004754 · Cited by 677 · see citing works
Hemesath, T. J., Steingrímsson, E., McGill, G., Hansen, M. J., Vaught, J., Hodgkinson, C. A., Arnheiter, H., Copeland, N. G., Jenkins, N. A., & Fisher, D. E. (1994) · Genes & Development · doi:10.1101/gad.8.22.2770 · Cited by 673 · see citing works
Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works
Micro-RNA speciation in fetal, adult and Alzheimer's disease hippocampus
Lukiw, W. J. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3280148e8b · Cited by 662 · see citing works
Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works
Carter, M. E., & Brunet, A. (2007) · Current Biology · doi:10.1016/j.cub.2007.01.008 · Cited by 581 · see citing works
Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
Jaunmuktane, Z., Mead, S., Ellis, M., Wadsworth, J. D. F., Nicoll, A. J., Kenny, J., Launchbury, F., Linehan, J., Richard-Loendt, A., Walker, A. S., et al. (2015) · Nature · doi:10.1038/nature15369 · Cited by 518 · see citing works
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 490 · see citing works
Dynein mutations impair autophagic clearance of aggregate-prone proteins
Ravikumar, B., Acevedo‐Arozena, A., Imarisio, S., Berger, Z., Vacher, C., O’Kane, C. J., Brown, S. D. M., & Rubinsztein, D. C. (2005) · Nature Genetics · doi:10.1038/ng1591 · Cited by 458 · see citing works
Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
Shibata, M., Lu, T., Furuya, T., Degterev, A., Mizushima, N., Yoshimori, T., MacDonald, M., Yankner, B., & Yuan, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600364200 · Cited by 458 · see citing works
Regulation of TFEB and V‐ATPases by mTORC1
Peña‐Llopis, S., Vega-Rubín-de-Celis, S., Schwartz, J. C., Wolff, N. C., Tran, T. A. T., Zou, L., Xie, X., Corey, D. R., & Brugarolas, J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.257 · Cited by 456 · see citing works
Tsunemi, T., Ashe, T. D., Morrison, B. E., Epilepsia, K. S., Au, J., Vázquez‐Roque, R. A., Lazarowski, E. R., Damian, V. A., Masliah, E., & Spada, A. R. L. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003799 · Cited by 440 · see citing works
Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429 · see citing works
Huntingtin functions as a scaffold for selective macroautophagy
Rui, Y.-N., Xu, Z., Patel, B., Chen, Z., Chen, D., Tito, A., David, G., Sun, Y., Stimming, E. F., Bellen, H. J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3101 · Cited by 423 · see citing works
Caughey, B. W., Raymond, G. J., Ernst, D. R., & Race, R. (1991) · Journal of Virology · doi:10.1128/jvi.65.12.6597-6603.1991 · Cited by 420 · see citing works
Mitochondria removal by autophagy
Wang, K., & Klionsky, D. J. (2011) · Autophagy · doi:10.4161/auto.7.3.14502 · Cited by 407 · see citing works
IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
Thompson, L. M., Aiken, C. T., Kaltenbach, L. S., Agrawal, N., Illes, K., Khoshnan, A., Martínez‐Vicente, M., Arrasate, M., O’Rourke, J. G., Khashwji, H., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200909067 · Cited by 396 · see citing works
Satoo, K., Noda, N. N., Kumeta, H., Fujioka, Y., Mizushima, N., Ohsumi, Y., & Inagaki, F. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.80 · Cited by 381 · see citing works
Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362 · see citing works
Purified and synthetic Alzheimer’s amyloid beta (Aβ) prions
Stöhr, J., Watts, J. C., Mensinger, Z. L., Oehler, A., Grillo, S. K., DeArmond, S. J., Prusiner, S. B., & Giles, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206555109 · Cited by 359 · see citing works
Genotype-phenotype correlations between GBA mutations and Parkinson disease risk and onset
Gan‐Or, Z., Giladi, N., Rozovski, U., Shifrin, C., Rosner, S., Gurevich, T., Bar‐Shira, A., & Orr‐Urtreger, A. (2008) · Neurology · doi:10.1212/01.wnl.0000304039.11891.29 · Cited by 359 · see citing works
Lee, J.-H., McBrayer, M. K., Wolfe, D. M., Haslett, L. J., Kumar, A., Sato, Y., Lie, P. P. Y., Mohan, P., Coffey, E. E., Kompella, U., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.050 · Cited by 358 · see citing works
Selective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB
Polito, V. A., Li, H., Martini‐Stoica, H., Wang, B., Li, Y., Xu, Y., Swartzlander, D. B., Palmieri, M., di Ronza, A., Lee, V. M. ‐., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201303671 · Cited by 350 · see citing works
Self-citationStimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343 · see citing works
Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease
Spampanato, C., Feeney, E., Li, L., Cardone, M., Lim, J., Annunziata, F., Zare, H., Polishchuk, R., Puertollano, R., Parenti, G., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201202176 · Cited by 341 · see citing works
Self-citationDoh‐ura, K., Iwaki, T., & Caughey, B. W. (2000) · Journal of Virology · doi:10.1128/jvi.74.10.4894-4897.2000 · Cited by 323 · see citing works
Sardi, S. P., Clarke, J. L., Kinnecom, C., Tamsett, T. J., Li, L., Stanek, L. M., Passini, M. A., Grabowski, G. A., Schlossmacher, M. G., Sidman, R. L., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108197108 · Cited by 319 · see citing works
MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5
Nezich, C. L., Wang, C., Fogel, A. I., & Youle, R. J. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201501002 · Cited by 309 · see citing works
Potential function for the Huntingtin protein as a scaffold for selective autophagy
Ochaba, J., Lukacsovich, T., Csikos, G., Zheng, S., Margulis, J., Salazar, L., Mao, K., Lau, A. L., Yeung, S. Y., Humbert, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420103111 · Cited by 308 · see citing works
Sevlever, D., Jiang, P., & Yen, S.-H. C. (2008) · Biochemistry · doi:10.1021/bi800699v · Cited by 305 · see citing works
Regulation of Neuronal Survival Factor MEF2D by Chaperone-Mediated Autophagy
Yang, Q., She, H., Gearing, M., Colla, E., Lee, M. K., Shacka, J. J., & Mao, Z. (2009) · Science · doi:10.1126/science.1166088 · Cited by 304 · see citing works
Autophagic degradation of tau in primary neurons and its enhancement by trehalose
Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297 · see citing works
Autophagosome targeting and membrane curvature sensing by Barkor/Atg14(L)
Fan, W., Nassiri, A., & Zhong, Q. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016472108 · Cited by 285 · see citing works
Lysosomal mTORC2/PHLPP1/Akt Regulate Chaperone-Mediated Autophagy
Arias, E., Koga, H., Díaz, A., Mocholí, E., Patel, B., & Cuervo, A. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.030 · Cited by 280 · see citing works
A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1
Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M. (2013) · Cell · doi:10.1016/j.cell.2013.07.030 · Cited by 275 · see citing works
Nath, S., Dancourt, J., Shteyn, V., Puente, G., Fong, W. M., Nag, S., Bewersdorf, J., Yamamoto, A., Antonny, B., & Melia, T. J. (2014) · Nature Cell Biology · doi:10.1038/ncb2940 · Cited by 269 · see citing works
Xiao, Q., Yan, P., Ma, X., Liu, H., Perez, R., Zhu, A., Gonzales, E., Burchett, J. M., Schuler, D. R., Cirrito, J. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3788-13.2014 · Cited by 266 · see citing works
Sardi, S. P., Clarke, J. L., Viel, C., Chan, M., Tamsett, T. J., Treleaven, C. M., Bu, J., Sweet, L., Passini, M. A., Dodge, J. C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220464110 · Cited by 252 · see citing works
Xiao, Q., Yan, P., Ma, X., Liu, H., Perez, R., Zhu, A., Gonzales, E. R., Tripoli, D. L., Czerniewski, L. R., Ballabio, A., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0705-15.2015 · Cited by 230 · see citing works
Self-citationMITF drives endolysosomal biogenesis and potentiates Wnt signaling in melanoma cells
Ploper, D., Taelman, V. F., Robert, L., Perez, B. S., Titz, B., Chen, H.-W., Graeber, T. G., von Euw, E., Ribas, A., & De Robertis, E. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424576112 · Cited by 228 · see citing works
Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice.
Ozcelik, S., Fraser, G., Castets, P., Schaeffer, V., Skachokova, Z., Breu, K., Clavaguera, F., Sinnreich, M., Kappos, L., Goedert, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062459 · Cited by 226 · see citing works
Autophagy induction by trehalose counter-acts cellular prion-infection
Aguib, Y., Heiseke, A., Gilch, S., Riemer, C., Baier, M., Ertmer, A., & Schätzl, H. M. (2009) · Autophagy · doi:10.4161/auto.5.3.7662 · Cited by 222 · see citing works
Kuiper, R. P. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg178 · Cited by 209 · see citing works
Coen, K., Flannagan, R. S., Baron, S., Carraro-Lacroix, L. R., Wang, D., Vermeire, W., Michiels, C., Munck, S., Baert, V., Sugita, S., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201201076 · Cited by 208 · see citing works
Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington's disease
Rose, C., Menzies, F. M., Renna, M., Acevedo‐Arozena, A., Corrochano, S., Sadiq, O., Brown, S. D. M., & Rubinsztein, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq093 · Cited by 200 · see citing works
Coffey, E. E., Beckel, J. M., Laties, A. M., & Mitchell, C. H. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.01.001 · Cited by 183 · see citing works
The p.L302P mutation in the lysosomal enzyme gene SMPD1 is a risk factor for Parkinson disease
Gan‐Or, Z., Ozelius, L. J., Bar‐Shira, A., Saunders-Pullman, R. J., Mirelman, A., Kornreich, R., Gana‐Weisz, M., Raymond, D., Rozenkrantz, L., Deik, A., et al. (2013) · Neurology · doi:10.1212/wnl.0b013e31828f180e · Cited by 177 · see citing works
Landel, V., Baranger, K., Virard, I., Loriod, B., Khrestchatisky, M., Rivera, S., Benech, P., & Féron, F. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-33 · Cited by 176 · see citing works
Quinacrine treatment trial for sporadic Creutzfeldt-Jakob disease
Geschwind, M. D., Kuo, A. L., Wong, K. S., Haman, A., Devereux, G., Raudabaugh, B., Johnson, D. Y., Torres-Chae, C. C., Finley, R., Garcia, P. A., et al. (2013) · Neurology · doi:10.1212/wnl.0b013e3182a9f3b4 · Cited by 172 · see citing works
Polyglutamine-expanded androgen receptor interferes with TFEB to elicit autophagy defects in SBMA
Cortés, C. J., Miranda, H. C., Frankowski, H., Batlevi, Y., Young, J. E., Le, A. T., Ivanov, N., Sopher, B. L., Carromeu, C., Muotri, A. R., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3787 · Cited by 164 · see citing works
Tiribuzi, R., Crispoltoni, L., Porcellati, S., Di Lullo, M., Florenzano, F., Pirro, M., Bagaglia, F., Kawarai, T., Zampolini, M., Orlacchio, A., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.08.003 · Cited by 162 · see citing works
Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer's disease brain
Rohn, T. T., Wirawan, E., Brown, R. J., Harris, J. R., Masliah, E., & Vandenabeele, P. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.11.003 · Cited by 160 · see citing works
Parr, C., Carzaniga, R., Gentleman, S., LEUVEN, F. V., Walter, J., & Sastre, M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00930-12 · Cited by 155 · see citing works
The elimination of accumulated and aggregated proteins: A role for aggrephagy in neurodegeneration
Yamamoto, A., & Simonsen, A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.08.015 · Cited by 152 · see citing works
Genetic and Chemical Activation of TFEB Mediates Clearance of Aggregated α-Synuclein
Kilpatrick, K., Zeng, Y., Hancock, T., & Segatori, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120819 · Cited by 143 · see citing works
TFEB regulates lysosomal proteostasis
Song, W., Wang, F., Savini, M., Ake, A., di Ronza, A., Sardiello, M., & Segatori, L. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt052 · Cited by 143 · see citing works
Fujioka, Y., Noda, N. N., Nakatogawa, H., Ohsumi, Y., & Inagaki, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.053520 · Cited by 143 · see citing works
The Role of Chaperone-Mediated Autophagy in Huntingtin Degradation
Qi, L., Zhang, X., Wu, J.-C., Lin, F., Wang, J., DiFiglia, M., & Qin, Z.-H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046834 · Cited by 138 · see citing works
Pogenberg, V., Ögmundsdóttir, M. H., Bergsteinsdóttir, K., Schepsky, A., Phung, B., Deineko, V., Milewski, M., Steingrímsson, E., & Wilmanns, M. (2012) · Genes & Development · doi:10.1101/gad.198192.112 · Cited by 137 · see citing works
Siddiqui, A., Bhaumik, D., Chinta, S. J., Rane, A., Rajagopalan, S., Lieu, C. A., Lithgow, G. J., & Andersen, J. K. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0109-15.2015 · Cited by 129 · see citing works
Zhang, X., Garbett, K., Veeraraghavalu, K., Wilburn, B., Gilmore, R., Mirnics, K., & Sisodia, S. S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0556-12.2012 · Cited by 122 · see citing works
2-Hydroxypropyl-β-cyclodextrin Promotes Transcription Factor EB-mediated Activation of Autophagy
Song, W., Wang, F., Lotfi, P., Sardiello, M., & Segatori, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.506246 · Cited by 109 · see citing works
Delivery of endosomes to lysosomes via microautophagy in the visceral endoderm of mouse embryos
Kawamura, N., Sun‐Wada, G., Aoyama, M., Harada, A., Takasuga, S., Sasaki, T., & Wada, Y. (2012) · Nature Communications · doi:10.1038/ncomms2069 · Cited by 108 · see citing works
Cortés, C. J., Qin, K., Cook, J., Solanki, A., & Mastrianni, J. A. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6189-11.2012 · Cited by 107 · see citing works
Rehli, M., den Elzen, N. R., Cassady, A. I., Ostrowski, M. C., & Hume, D. A. (1999) · Genomics · doi:10.1006/geno.1998.5588 · Cited by 95 · see citing works
Antiprion immunotherapy: to suppress or to stimulate?
Aguzzi, A., & Sigurdson, C. J. (2004) · Nature reviews. Immunology · doi:10.1038/nri1437 · Cited by 78 · see citing works
Dynamics and function of PtdIns(3) P in autophagy
Obara, K., & Ohsumi, Y. (2008) · Autophagy · doi:10.4161/auto.6790 · Cited by 72 · see citing works
Tsujimura, A., Taguchi, K., Watanabe, Y., Tatebe, H., Tokuda, T., Mizuno, T., & Tanaka, M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.10.011 · Cited by 67 · see citing works
The Golgi as a potential membrane source for autophagy
Geng, J., & Klionsky, D. J. (2010) · Autophagy · doi:10.4161/auto.6.7.13009 · Cited by 65 · see citing works
Michell, A. W., Tofaris, G. K., Gossage, H., Tyers, P., Spillantini, M. G., & Barker, R. (2007) · Cell Transplantation · doi:10.3727/000000007783464911 · Cited by 63 · see citing works
Xu, Y., Tian, C., Wang, S.-B., Xie, W.-L., Guo, Y., Zhang, J., Shi, Q., Chen, C., & Dong, X. (2012) · Autophagy · doi:10.4161/auto.21482 · Cited by 62 · see citing works
Self-citationStimulation of ATG12-ATG5 Conjugation by Ribonucleic Acid
Shao, Y., Gao, Z., Feldman, T., & Jiang, X. (2007) · Autophagy · doi:10.4161/auto.3270 · Cited by 50 · see citing works
Structural insights into E2–E3 interaction for LC3 lipidation
Metlagel, Z., Otomo, C., Ohashi, K., Takaesu, G., & Otomo, T. (2014) · Autophagy · doi:10.4161/auto.27594 · Cited by 29 · see citing works
De Novo Prion Aggregates Trigger Autophagy in Skeletal Muscle
Joshi-Barr, S., Bett, C. K., Chiang, W.-C. J., Trejo, M., Goebel, H. H., Sikorska, B., Liberski, P. P., Raeber, A. J., Lin, J. H., Masliah, E., et al. (2013) · Journal of Virology · doi:10.1128/jvi.02279-13 · Cited by 20 · see citing works
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Lysosomes as dynamic regulators of cell and organismal homeostasis
Ballabio, A., & Bonifacino, J. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0185-4 · Cited by 1,469 · see citing works
Self-citationTargeted protein degradation: mechanisms, strategies and application
Zhao, L., Zhao, J., Zhong, K., Tong, A., & Jia, D. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00966-4 · Cited by 986 · see citing works
Lysosomes as a therapeutic target
Bonam, S. R., Wang, F., & Muller, S. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0036-1 · Cited by 764 · see citing works
“TFEB has received particular attention in this regard [193] [194] [195] , with recent data suggesting that TFEB is selectively lost in patients with AD (as well as ALS) 196 .”
BackgroundAutophagy: The spotlight for cellular stress responses
Ravanan, P., Florance, I., & Talwar, P. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.08.029 · Cited by 578 · see citing works
Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400 · see citing works
Role of lysosomes in physiological activities, diseases, and therapy
Zhang, Z., Yue, P., Lu, T., Wang, Y., Wei, Y., & Wei, X. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01087-1 · Cited by 364 · see citing works
“The autophagylysosome pathway (ALP) is essential for the survival of non-dividing neurons by contributing to the removal of abnormal large protein aggregates and organelles [76, 77].”
BackgroundSelective autophagy as a potential therapeutic target for neurodegenerative disorders
Scrivo, A., Bourdenx, M., Pampliega, O., & Cuervo, A. M. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30238-2 · Cited by 355 · see citing works
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3
Paquette, M., El–Houjeiri, L., Zirden, L. C., Puustinen, P., Blanchette, P., Jeong, H., Dejgaard, K., Siegel, P. M., & Pause, A. (2021) · Autophagy · doi:10.1080/15548627.2021.1898748 · Cited by 260 · see citing works
“Interestingly, TFEB and TFE3 also play important roles in non-dividing neurons to clear toxins and misfolded proteins through regulation of autophagic pathways [17].”
BackgroundAutophagy Induction as a Therapeutic Strategy for Neurodegenerative Diseases
Djajadikerta, A., Keshri, S., Tanasa, M. P., Prestil, R., Ryan, L., & Rubinsztein, D. C. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.035 · Cited by 238 · see citing works
“[141] Martini-Stoica H, Xu Y, Ballabio A, Zheng H.”
Wang, Y., Cheng, H., Wang, T., Zhang, K., Zhang, Y., & Kang, X. (2023) · Cell Proliferation · doi:10.1111/cpr.13448 · Cited by 239 · see citing works
“(TFEB) is the main transcription regulator of lysosome and autophagy genes.(168) Apigenin can promote the nuclear translocation of TFEB by”
BackgroundSTUB1 regulates TFEB‐induced autophagy–lysosome pathway
Sha, Y., Rao, L., Settembre, C., Ballabio, A., & Eissa, N. T. (2017) · The EMBO Journal · doi:10.15252/embj.201796699 · Cited by 231 · see citing works
“Methods to induce TFEB activation to enhance autophagy – lysosome-mediated degradation of misfolded proteins have been suggested for treatment of diseases associated with misfolded proteins such as neurodegenerative diseases (Decressac & Bjo¨rklund, 2013; Martini-Stoica et al , 2016).”
Self-citationZhang, W., Xu, C., Sun, J., Shen, H., Wang, J., & Yang, C. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.008 · Cited by 213 · see citing works
Autophagy in aging and longevity
Wong, S. Q., Kumar, A. V., Mills, J., & Lapierre, L. R. (2019) · Human Genetics · doi:10.1007/s00439-019-02031-7 · Cited by 204 · see citing works
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 · see citing works
Dysregulation of autophagy as a common mechanism in lysosomal storage diseases
Seranova, E., Connolly, K. J., Zatyka, M., Rosenstock, T. R., Barrett, T. G., Tuxworth, R. I., & Sarkar, S. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170055 · Cited by 175 · see citing works
Zheng, X., Lin, W., Jiang, Y., Lu, K., Wei, W., Huo, Q., Cui, S., Yang, X., Li, M., Xu, N., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1886720 · Cited by 167 · see citing works
The Lysosome Signaling Platform: Adapting With the Times
Inpanathan, S., & Botelho, R. J. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00113 · Cited by 157 · see citing works
The Role of Cathepsin D in the Pathogenesis of Human Neurodegenerative Disorders
Vidoni, C., Follo, C., Savino, M., Melone, M. A. B., & Isidoro, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21394 · Cited by 164 · see citing works
Autophagy in Bone Remodeling: A Regulator of Oxidative Stress
Zhu, C., Shen, S., Zhang, S., Huang, M., Zhang, L., & Chen, X. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.898634 · Cited by 166 · see citing works
Xu, Y., Propson, N. E., Du, S., Xiong, W., & Zheng, H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2023418118 · Cited by 171 · see citing works
Self-citationLysosomes in senescence and aging
Tan, J. X., & Finkel, T. (2023) · EMBO Reports · doi:10.15252/embr.202357265 · Cited by 160 · see citing works
Victoria, G. S., & Zurzolo, C. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701047 · Cited by 150 · see citing works
“Lysosomal stress can also alter TFEB signaling, which is directly responsible for increasing lysosomal exocytosis (Martini-Stoica et al., 2016).”
BackgroundZhu, L., Yuan, Y., Yuan, L., Li, L., Liu, F., Liu, J., Chen, Y., Lu, Y., & Cheng, J. (2020) · Theranostics · doi:10.7150/thno.44051 · Cited by 153 · see citing works
“TFEB is a known master transcriptional regulator of autophagy and can regulate lysosome biogenesis and promote autophagosome-lysosome activity by binding to the CLEAR element on a variety of autophagy and lysosomal genes to induce their expression [41, 42].”
BackgroundIssa, A.-R., Sun, J., Petitgas, C., Mesquita, A., Dulac, A., Robin, M., Mollereau, B., Jenny, A., Chérif‐Zahar, B., & Birman, S. (2018) · Autophagy · doi:10.1080/15548627.2018.1491489 · Cited by 152 · see citing works
Chandra, S., Roy, A., Jana, M., & Pahan, K. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.12.007 · Cited by 149 · see citing works
Autophagy impairment in Parkinson’s disease
Karabiyik, C., Lee, M. J., & Rubinsztein, D. C. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170023 · Cited by 137 · see citing works
“Translocation of TFEB to the nucleus enables its transcriptional activity, autophagosome formation and autophagosome-lysosome fusion (16).”
BackgroundHoller, C. J., Taylor, G., Deng, Q., & Kukar, T. L. (2017) · eNeuro · doi:10.1523/eneuro.0100-17.2017 · Cited by 133 · see citing works
“Lysosome dysfunction is a common occurrence in numerous neurodegenerative diseases (Platt et al., 2012; Martini-Stoica et al., 2016) and growing evidence indicates a critical role for PGRN in the maintenance of lysosome homeostasis (Ahmed et al.”
BackgroundChandra, S., Jana, M., & Pahan, K. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.0054-18.2018 · Cited by 134 · see citing works
“Lysosomal adaptation under different physiological and pathological scenarios is dependent on a regulatory gene network known as CLEAR (coordinated lysosomal expression and regulation), with the master regulator TFEB at its core (Sardiello et al., 2009; Martini-Stoica et al., 2016).”
BackgroundIyaswamy, A., Thakur, A., Guan, X.-J., Krishnamoorthi, S., Fung, T. Y., Lu, K., Gaurav, I., Yang, Z., Su, C.-F., Lau, K.-F., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01657-4 · Cited by 134 · see citing works
“28,29 Interestingly, a relationship between exosomes and autophagy that is considered a key protein degradation pathway functioning to clear misfolded proteins in various neurodegenerative diseases including AD, has been studied.”
BackgroundExercise activates lysosomal function in the brain through AMPK‐SIRT1‐TFEB pathway
Huang, J., Wang, X., Zhu, Y., Li, Z., Zhu, Y., Wu, J., Qin, Z., Xiang, M., & Lin, F. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13114 · Cited by 129 · see citing works
Xu, Y., Du, S., Marsh, J. A., Horie, K., Sato, C., Ballabio, A., Karch, C. M. M., Holtzman, D. M., & Zheng, H. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0738-0 · Cited by 121 · see citing works
Self-citationPost-translational modifications: Regulators of neurodegenerative proteinopathies
Gupta, R. V., Sahu, M., Srivastava, D., Tiwari, S., Ambasta, R. K., & Kumar, P. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101336 · Cited by 124 · see citing works
Members, E. W. E., Terron, A., Bal-Price, A., Paini, A., Monnet-Tschudi, F., Bennekou, S. H., Leist, M., & Schildknecht, S. (2018) · Archives of Toxicology · doi:10.1007/s00204-017-2133-4 · Cited by 124 · see citing works
“The two main systems for the removal of misfolded proteins are: (1) the autophagy–lysosomal pathway (ALP), which removes dysfunctional proteins, aggregates, and even subcellular organelles; and (2) the ubiquitin proteasomal system (UPS), which catalyzes the tagging of target proteins by ubiquitination, followed by the…”
BackgroundRegulated cell death: discovery, features and implications for neurodegenerative diseases
Cui, J., Zhao, S., Li, Y., Zhang, D., Wang, B., Xie, J., & Wang, J. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00799-8 · Cited by 125 · see citing works
“Deficiencies in the autophagy-lysosomal pathway can contribute to the aggregation of abnormal protein, the generation of toxic substances and the accumulation of dysfunctional organelles [149].”
BackgroundZhang, Z., Yan, J., Bowman, A. B., Bryan, M. R., Singh, R., & Aschner, M. (2019) · Autophagy · doi:10.1080/15548627.2019.1688488 · Cited by 116 · see citing works
Roles of Autophagy-Related Genes in the Pathogenesis of Inflammatory Bowel Disease
Kim, S., Eun, H. S., & Jo, E. (2019) · Cells · doi:10.3390/cells8010077 · Cited by 120 · see citing works
A Self-Assembled α-Synuclein Nanoscavenger for Parkinson’s Disease
Liu, J., Liu, C., Zhang, J., Zhang, Y., Liu, K., Song, J., Sreenivasmurthy, S. G., Wang, Z., Shi, Y., Chu, C., et al. (2020) · ACS Nano · doi:10.1021/acsnano.9b06453 · Cited by 116 · see citing works
Gao, L., Li, X., Meng, S., Ma, T., Wan, L., & Xu, S. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s235969 · Cited by 115 · see citing works
Targeting Autophagy to Overcome Human Diseases
Condello, M., Pellegrini, E., Caraglia, M., & Meschini, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030725 · Cited by 113 · see citing works
“The EB transcription factor (TFEB) has been identified as the factor that positively regulates genes related to formation of autophagosomes and the lysosome fusion, increasing the clearance of lysosomal exocytosis [104].”
BackgroundYang, C., Su, C.-F., Iyaswamy, A., Krishnamoorthi, S. K., Zhu, Z., Yang, S., Tong, B. C., Liu, J., Sreenivasmurthy, S. G., Guan, X., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.017 · Cited by 112 · see citing works
Autophagy–lysosomal-associated neuronal death in neurodegenerative disease
Nixon, R. A. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02799-7 · Cited by 117 · see citing works
“…controlling the “CLEAR Network” of genes encoding autophagy and especially lysosomal biogenesis constitutes a successful strategy to delay effects of cell aging or extend longevity in vivo in aging models [179] and to slow or prevent neurodegenerative disease progression in mouse models [149].”
Liu, Y., Zhou, H., Yin, T., Gong, Y., Yuan, G., Chen, L., & Liu, J. (2019) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2019.05.066 · Cited by 111 · see citing works
Penke, B., Bogár, F., Crul, T., Sántha, M., Tóth, M. E., & Vı́gh, L. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010325 · Cited by 106 · see citing works
“The first step is the formation of a crescent-shaped double membrane (phagophore or isolation membrane) derived from multiple sources, such as cytoplasmic membrane, mitochondria, or ER- and Golgi apparatus [96,122].”
BackgroundTFEB–vacuolar ATPase signaling regulates lysosomal function and microglial activation in tauopathy
Wang, B., Martini‐Stoica, H., Qi, C., Lu, T., Wang, S., Xiong, W., Qi, Y., Xu, Y., Sardiello, M., Li, H., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01494-2 · Cited by 106 · see citing works
“Lysosomes play essential roles in cellular homeostasis through the LYNUS system and the coordinated mTOR-TFEB lysosome to nucleus signaling 24 .”
Self-citationRen, H., Zhai, W., Lu, X., & Wang, G. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.691881 · Cited by 101 · see citing works
Genetic, Structural, and Functional Evidence Link TMEM175 to Synucleinopathies
Krohn, L., Öztürk, T. N., Vanderperre, B., Bencheikh, B. O. A., Ruskey, J. A., Laurent, S. B., Spiegelman, D., Postuma, R. B., Arnulf, I., Hu, M. T. M., et al. (2019) · Annals of Neurology · doi:10.1002/ana.25629 · Cited by 103 · see citing works
“The autophagy lysosomal pathway (ALP) likely plays a major role in PD pathogenesis,(4) as deficits in the ALP may lead to α-synuclein aggregation and accumulation and reduction in glucocerebrosidase (GCase) activity.(5) GCase is encoded by GBA, which harbors variants that are among the most common risk factors for PD.”
BackgroundAn FGF15/19-TFEB regulatory loop controls hepatic cholesterol and bile acid homeostasis
Wang, Y., Gunewardena, S., Li, F., Matye, D. J., Chen, C., Chao, X., Jung, T., Zhang, Y., Czerwiński, M., Ni, H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17363-6 · Cited by 99 · see citing works
Rakshe, P. S., Dutta, B. J., Chib, S., Maurya, N., & Singh, S. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102255 · Cited by 103 · see citing works
Cai, Y., Yang, L., Hu, G.-K., Chen, X., Niu, F., Yuan, L., Liu, H., Xiong, H., Arikkath, J., & Buch, S. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201605065 · Cited by 102 · see citing works
“Our understanding of the link between autophagy and synaptic structure and function in absence of neurodegeneration (Menzies et al., 2015; Martini-Stoica et al., 2016) has been limited.”
BackgroundTFEB protects nucleus pulposus cells against apoptosis and senescence via restoring autophagic flux
Zheng, G., Pan, Z., Zhan, Y., Tang, Q., Zheng, F., Zhou, Y., Wu, Y., Zhou, Y., Chen, D., Chen, J., et al. (2018) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2018.10.011 · Cited by 97 · see citing works
Caberlotto, L., Nguyen, T.-P., Lauria, M., Priami, C., Rimondini, R., Maioli, S., Cedazo-Mı́nguez, Á., Sita, G., Morroni, F., Corsi, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-39828-5 · Cited by 97 · see citing works
Zhang, H., Ni, W., Yu, G., Geng, Y., Lou, J., Qi, J., Chen, Y., Li, F., Ye, H., Ma, H., et al. (2023) · Theranostics · doi:10.7150/thno.78370 · Cited by 96 · see citing works
“Transcription factor EB (TFEB), which is a component of the microphthalmia transcription factor family, is considered a master modulator of autophagy activity and lysosome biogenesis [28].”
BackgroundKrohn, L., Heilbron, K., Blauwendraat, C., Reynolds, R. H., Yu, E., Senkevich, K. A., Rudakou, U., Estiar, M. A., Gustavsson, E. K., Brolin, K. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34732-5 · Cited by 101 · see citing works
TFEB, a potential therapeutic target for osteoarthritis via autophagy regulation
Zheng, G., Zhan, Y., Li, X., Pan, Z., Zheng, F., Zhang, Z., Zhou, Y., Wu, Y., Wang, X., Gao, W., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0909-y · Cited by 94 · see citing works
Li, C., Wang, X., Li, X., Qiu, K., Jiao, F., Liu, Y., Kong, Q., Liu, Y., & Wu, Y. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00170 · Cited by 90 · see citing works
Emerging pathways driving early synaptic pathology in Alzheimer's disease
Briggs, C. A., Chakroborty, S., & Stutzmann, G. E. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.088 · Cited by 91 · see citing works
“Lysosome dysfunction is implicated along multiple lines of evidence in neurodegenerative disease - AD, Parkinson’s Disease and Huntington’s Disease in particular [13,32,48,65,72,93,119].”
BackgroundTherapeutic role of sirtuins in neurodegenerative disease and their modulation by polyphenols
Ajami, M., Pazoki–Toroudi, H., Amani, H., Nabavi, S. F., Braidy, N., Vacca, R. A., Atanasov, A. G., MOCAN, A., & Nabavi, S. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.022 · Cited by 91 · see citing works
“ALP impairment esults in aggregation of toxic protein species, and accumulation f damaged organelles such as dysfunctional mitochondria that ead to development and progression of neurodegenerative disorers (Martini-Stoica et al., 2016).”
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 · see citing works
Targeting Undruggable Transcription Factors with PROTACs: Advances and Perspectives
Li, Y., Song, J. H., Zhou, P., Zhou, J., & Xie, S. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00691 · Cited by 88 · see citing works
Recent advances in organelle-targeted organic photosensitizers for efficient photodynamic therapy
Dirak, M., Yenici, C. M., & Kölemen, S. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.215710 · Cited by 88 · see citing works
Xu, Y., Ren, J., He, X., Chen, H., Wei, T., & Feng, W. (2019) · Autophagy · doi:10.1080/15548627.2019.1569928 · Cited by 87 · see citing works
Self-citationTranscription factor EB overexpression prevents neurodegeneration in experimental synucleinopathies
Arotçarena, M.-L., Bourdenx, M., Dutheil, N., Thiolat, M.-L., Doudnikoff, É., Doveró, S., Ballabio, A., Fernagut, P., Meissner, W. G., Bézard, E., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.129719 · Cited by 82 · see citing works
“Since TFEB is a master gene in the regulation of ALP (17–20, 22), we Because alteration of lysosomal integrity, and lysosomal membrane permeabilization especially, have been described in synucleinopathies (38, 39), we next explored whether overexpression of TFEB could rescue lysosomal membrane…”
Self-citationKim, J. H., Yu, D.-H., Huh, Y. H., Lee, E., Kim, H., & Kim, H. R. (2017) · Scientific Reports · doi:10.1038/srep41129 · Cited by 84 · see citing works
Jarazo, J., Barmpa, K., Modamio, J., Saraiva, C., Sabaté‐Soler, S., Rosety, I., Griesbeck, A., Skwirblies, F., Zaffaroni, G., Smits, L. M., et al. (2021) · Movement Disorders · doi:10.1002/mds.28810 · Cited by 96 · see citing works
“compound HP-β-CD was reported to modulate autophagy by increasing TFEB nuclear translocation in human neuroglioma cells.(29,35,36) Treatment with HPβ-CD during the entire differentiation process was able to increase the proportion of nuclei that colocalized with TFEB in a two-dimensional neuronal culture at 21 days of…”
BackgroundResultLysosomal stress response (LSR): Physiological importance and pathological relevance
Lakpa, K. L., Khan, N., Afghah, Z., Chen, X.-S., & Geiger, J. (2021) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-021-09990-7 · Cited by 70 · see citing works
Pi, H., Li, M., Tian, L., Yang, Z., Yu, Z., & Zhou, Z. (2017) · Scientific Reports · doi:10.1038/srep43466 · Cited by 80 · see citing works
Li, X., Zhang, X., Zheng, L., Kou, J., Zhong, Z., Jiang, Y., Wang, W., Dong, Z., Liu, Z., Han, X. B., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.433 · Cited by 79 · see citing works
“Transcription factor EB (TFEB) is a recently discovered key regulator of autophagy-lysosome pathway to promote protein clearance.(25,41) TFEB could upregulate the expression of nearly two-thirds of autophagy-”
BackgroundTFEB is a master regulator of tumor-associated macrophages in breast cancer
Li, Y., Hodge, J., Liu, Q., Wang, J., Wang, Y., Evans, T. D., Altomare, D., Yao, Y., Murphy, E. A., Razani, B., et al. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2020-000543 · Cited by 81 · see citing works
Targeting α-Synuclein for PD Therapeutics: A Pursuit on All Fronts
Teil, M., Arotçarena, M.-L., Faggiani, E., Laferrière, F., Bézard, E., & Dehay, B. (2020) · Biomolecules · doi:10.3390/biom10030391 · Cited by 78 · see citing works
Targeting autophagy in Alzheimer’s disease: Animal models and mechanisms
Zhang, X.-W., 澳门大学中华医药研究院中药质量研究国家重点实验室, 澳. 凼. 9., State Key Laboratory of Quality Research in Chinese Medicine, I. O. C. M. S., Zhu, X.-X., Tang, D.-S., Lu, J.-H., 佛山大学广东省动物分子设计与精准育种重点实验室, 广., & Guangdong Provincial Key Laboratory of Animal Molecular Design and Precise Breeding, G. E. T. C. O. G. P. (2023) · Zoological Research · doi:10.24272/j.issn.2095-8137.2023.294 · Cited by 77 · see citing works
TFEB/Mitf links impaired nuclear import to autophagolysosomal dysfunction in C9-ALS
Cunningham, K. M., Maulding, K., Ruan, K., Şentürk, M., Grima, J. C., Sung, H., Zuo, Z., Song, H., Gao, J., Dubey, S. K., et al. (2020) · eLife · doi:10.7554/elife.59419 · Cited by 75 · see citing works
Yadavalli, N., & Ferguson, S. M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2303789120 · Cited by 75 · see citing works
Trivedi, P. C., Bartlett, J. J., Perez, L. J., Brunt, K. R., Legare, J. F., Hassan, A., Kienesberger, P. C., & Pulinilkunnil, T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.09.004 · Cited by 73 · see citing works
Brijmohan, A. S., Batchu, S. N., Majumder, S., Alghamdi, T. A., Thieme, K., McGaugh, S., Liu, Y., Advani, S. L., Bowskill, B. B., Kabir, M. G., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00034 · Cited by 71 · see citing works
“Cellular stress inactivates mTORC1, leading to dephosphorylation of TFEB, its release from 14-3-3 proteins and translocation of the transcription factor to the nucleus (Settembre et al., 2011; Martini-Stoica et al., 2016).”
BackgroundBodas, M., Patel, N., Silverberg, D., Walworth, K., & Vij, N. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6842 · Cited by 70 · see citing works
“The aberrant expression/activity of TFEB is evident in several pathological conditions, especially in age-related degenerative or lysosomal storage disorders, where TFEB impairment leads to accumulation of misfolded or damaged proteins in aggresome-bodies (34, 47).”
Grimm, C. M., Butz, E. S., Chen, C., Wahl‐Schott, C., & Biel, M. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.04.003 · Cited by 68 · see citing works
Xu, Y., Zhang, S., & Zheng, H. (2018) · Autophagy · doi:10.1080/15548627.2018.1532258 · Cited by 69 · see citing works
“The autophagy-lysosomal pathway (ALP) is a highly conserved degradation pathway that acts by engulfing cellular substrates within MAP1LC3B/LC3B (microtubule-associated protein 1 light chain 3 beta)-positive double-membrane autophagosomes before delivering them to the lysosome for eventual degradation [5,6].”
BackgroundSelf-citationMitochondria–lysosome membrane contacts are defective in GDAP1-related Charcot–Marie–Tooth disease
Cantarero, L., Juárez‐Escoto, E., Civera-Tregón, A., Rodríguez-Sanz, M., Roldán, M., Benítez, R., Hoenicka, J., & Palau, F. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa243 · Cited by 67 · see citing works
Yin, Y., Tian, B., Li, X., Yu, Y.-C., Deng, D., Sun, L., Qu, H., Wu, R., Xu, X., Sun, H., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121743 · Cited by 67 · see citing works
Adiponectin alleviated Alzheimer‐like pathologies via autophagy‐lysosomal activation
He, K., Nie, L., Ali, T., Wang, S., Chen, X., Liu, Z., Li, W., Zhang, K., Xu, J., Liu, J., et al. (2021) · Aging Cell · doi:10.1111/acel.13514 · Cited by 65 · see citing works
The fluorescence toolbox for visualizing autophagy
Ding, S., & Hong, Y. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00913j · Cited by 63 · see citing works
TFEB in Alzheimer's disease: From molecular mechanisms to therapeutic implications
Gu, Z., Cao, H., Zuo, C., Huang, Y., Miao, J., Song, Y., Yang, Y., Zhu, L., & Wang, F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105855 · Cited by 63 · see citing works
“Recently, studies have demonstrated the roles of TFEB and ALP dysfunction in the development of several neurodegenerative diseases, including AD (Boland et al., 2018; Martini-Stoica et al., 2016; Song et al., 2021).”
BackgroundNatural products for the treatment of neurodegenerative diseases
Cui, D., Chen, Y., Ye, B., Guo, W., Wang, D., & He, J. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155101 · Cited by 63 · see citing works
Yuan, Y., Li, L., Zhu, L., Liu, F., Tang, X., Liao, G., Liu, J., Cheng, J., Chen, Y., & Lu, Y. (2020) · Stem Cells · doi:10.1002/stem.3144 · Cited by 63 · see citing works
“TFEB activity is regulated by mTORC1-mediated phosphorylation at specific serine residues in response to changes in nutritional status.(16)”
BackgroundSu, C., Feng, Y. Y., Liu, T., Liu, X., Bao, J., Shi, A., Hu, D., Liu, T., & Yu, Y. (2017) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12721 · Cited by 61 · see citing works
Snouwaert, J. N., Church, R. J., Jania, L. A., Nguyen, M., Wheeler, M. L., Saintsing, A., Mieczkowski, P. A., de Villena, F. P., Armao, D. M., Moy, S. S., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.118 · Cited by 61 · see citing works
“, 2016), Alzheimer’s disease (Martini-Stoica et al., 2016), amyotrophic lateral sclerosis (ALS) (Kiriyama and Nochi, 2015), hereditary spastic paraplegia (HSP) (Ebrahimi-Fakhari et al.”
BackgroundLiu, L., Tao, Z., Zheng, L., Brooke, J., Smith, C., Liu, D., Long, Y. C., & Cheng, Z. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2016.66 · Cited by 61 · see citing works
Melatonin as an endogenous regulator of diseases: The role of autophagy
Roohbakhsh, A., Shamsizadeh, A., Hayes, A. W., Reiter, R. J., & Karimi, G. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.01.022 · Cited by 59 · see citing works
Yang, C., Zhu, Z., Tong, B. C., Iyaswamy, A., Xie, W.-J., Zhu, Y., Sreenivasmurthy, S. G., Krishnamoorthi, S., Cheung, K., Song, J., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101445 · Cited by 60 · see citing works
Phillipson, O. T. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.09.006 · Cited by 60 · see citing works
Yuan, L., Yuan, Y., Liu, F., Li, L., Liu, J., Chen, Y., Cheng, J., & Lu, Y. (2021) · Aging · doi:10.18632/aging.202653 · Cited by 59 · see citing works
“Studies have demonstrated that TFEB promotes the expression of genes in the autophagy pathway, as well as genes encoding the components of lysosomes [29, 50, 51].”
BackgroundThe Role and Regulatory Mechanism of Transcription Factor EB in Health and Diseases
Zhu, S., Yao, R.-Q., Li, Y., Zhao, P., Ren, C., Du, X., & Yao, Y.-M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.667750 · Cited by 56 · see citing works
“The activation and translocation of TFEB are sequentially initiated under exposure of cellular stress, such as starvation and lysosomal dysfunction (Martina et al., 2012; Roczniak-Ferguson et al., 2012; Medina et al., 2015).”
BackgroundInfluentialTranscription factor EB: an emerging drug target for neurodegenerative disorders
Song, J., Liu, J., Jiang, Y., Wang, Z., & Li, M. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.10.013 · Cited by 59 · see citing works
Treadmill exercise reduces α-synuclein spreading via PPARα
Dutta, D., Paidi, R. K., Raha, S., Roy, A., Chandra, S., & Pahan, K. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111058 · Cited by 57 · see citing works
Zeng, X., Li, P., Ning, Y., Zhao, Y., Peng, Y., Yang, N., Zhao, Z., Chen, J., & Zhou, Y. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0316-4 · Cited by 57 · see citing works
Autophagy in exposure to environmental chemicals
Pesonen, M., & Vähäkangas, K. (2019) · Toxicology Letters · doi:10.1016/j.toxlet.2019.01.007 · Cited by 57 · see citing works
Mao, X., Lei, H., Yi, T., Su, P., Tang, S., Tong, Y., Dong, B., Ruan, G., Mustea, A., Sehouli, J., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02211-2 · Cited by 55 · see citing works
“TFEB downregulation or deficiency can obviously affect the cellular phenotype in a physiologically relevant manner in settings including atherosclerosis [26], nonalcoholic fatty liver disease [27], cancer [28] and neurodegeneration [29].”
BackgroundMaterial properties of phase-separated TFEB condensates regulate the autophagy-lysosome pathway
Wang, Z., Chen, D., Guan, D., Liang, X., Xue, J., Zhao, H., Song, G., Lou, J., He, Y., & Zhang, H. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202112024 · Cited by 53 · see citing works
Pircs, K., Drouin‐Ouellet, J., Horváth, V., Gil, J., Rezeli, M., Garza, R., Grassi, D. A., Sharma, Y., St‐Amour, I., Harris, K. L., et al. (2021) · Brain · doi:10.1093/brain/awab473 · Cited by 53 · see citing works
Cui, Y., Arnold, F. J., Peng, F., Wang, D., Li, J. S., Michels, S., Wagner, E. J., Spada, A. R. L., & Li, W. (2023) · Nature Communications · doi:10.1038/s41467-023-36311-8 · Cited by 50 · see citing works
- Authors
- Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H.
- Affiliations
- Baylor College of Medicine (US)
- Corresponding author
- Zheng, Hui
- Venue
- Trends in Neurosciences
- Publisher
- Elsevier BV
- Published
- 2016-04
- Volume
- 39
- Issue
- 4
- Pages
- 221-234
- ISSN
- 0166-2236 (ISSN-L)
- PMC
- PMC4928589
- OpenAlex
- W2293027573
- Cited by
- 436
- References
- 127
- Citations by year
- 2026: 38 · 2025: 41 · 2024: 46 · 2023: 65 · 2022: 48 · 2021: 53 · 2020: 43 · 2019: 34 · 2018: 27 · 2017: 31 · 2016: 10
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Neurosciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (RF1AG020670, F30AG050412, R01AG020670)
- National Institute of Neurological Disorders and Stroke (R01NS076117, RF1NS093652, R01NS078072, R01NS093652)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- autophagy-lysosome pathway, TFEB, neurodegenerative diseases, lysosomal biogenesis, protein aggregation, Alzheimer's disease, Parkinson's disease, Huntington's disease, prion disease, autophagy regulation, therapeutic target
- MeSH terms
- Animals, Autophagy, Brain, Humans, Lysosomes, Nerve Degeneration, Neurodegenerative Diseases, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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