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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 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]
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“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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,920
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
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,788
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
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 1,683
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
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
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 1,491
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 1,452
Self-citationRoczniak-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 1,393
Itakura, E., Kishi‐Itakura, C., & Mizushima, N. (2012) · Cell · doi:10.1016/j.cell.2012.11.001 · Cited by 1,385
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
Self-citationMTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
Martina, J. A., Chen, Y., Gucek, M., & Puertollano, R. (2012) · Autophagy · doi:10.4161/auto.19653 · Cited by 1,333
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
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
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
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
Self-citationRogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992
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
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
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
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
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 905
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
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
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
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
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851
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
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
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
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
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
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 757
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
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 729
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
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
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
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
Carter, M. E., & Brunet, A. (2007) · Current Biology · doi:10.1016/j.cub.2007.01.008 · Cited by 588
Micro-RNA speciation in fetal, adult and Alzheimer's disease hippocampus
Lukiw, W. J. (2007) · NeuroReport · doi:10.1097/wnr.0b013e3280148e8b · Cited by 530
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
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 514
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 472
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
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 456
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
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
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
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 416
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 415
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 384
Mitochondria removal by autophagy
Wang, K., & Klionsky, D. J. (2011) · Autophagy · doi:10.4161/auto.7.3.14502 · Cited by 380
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 375
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 363
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
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
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 356
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
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
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
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 321
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 312
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
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
Sevlever, D., Jiang, P., & Yen, S.-H. C. (2008) · Biochemistry · doi:10.1021/bi800699v · Cited by 305
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
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 291
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
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 279
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
Pickford, F., Masliah, E., Britschgi, M., Lucin, K., 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 268
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
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
Xiao, Q., Yan, P., Ma, X., Liu, H., Perez, R., Zhu, A., Gonzales, E., Tripoli, D. L., Czerniewski, L., Ballabio, A., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.0705-15.2015 · Cited by 238
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
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
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
Kuiper, R. P. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg178 · Cited by 209
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
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 202
Coffey, E. E., Beckel, J. M., Laties, A. M., & Mitchell, C. H. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.01.001 · Cited by 191
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 179
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
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
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
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
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 161
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 155
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
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 145
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
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
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
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 136
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 130
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
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 115
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 113
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
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
Antiprion immunotherapy: to suppress or to stimulate?
Aguzzi, A., & Sigurdson, C. J. (2004) · Nature reviews. Immunology · doi:10.1038/nri1437 · Cited by 78
Dynamics and function of PtdIns(3) P in autophagy
Obara, K., & Ohsumi, Y. (2008) · Autophagy · doi:10.4161/auto.6790 · Cited by 72
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
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 66
Self-citationThe 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
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
Stimulation 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
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
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
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“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 .”
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Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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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