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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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“In contrast, the lysosomal pathway degrades long-lived proteins, protein aggregates, and even entire organelles through processes like endocytosis and autophagy (Martini-Stoica et al., 2016; Wang et al., 2019).”
O’Brien, T. J., Navarro, E. L., Barroso, C., Menzies, L. A., Martínez-Pérez, E., Carling, D., & Brown, A. E. (2025) · BMC Biology · doi:10.1186/s12915-025-02368-8 · Cited by 1
“…many neurodegenerative disorders [56] including: Hermansky-Pudlak Syndrome [57], hereditary spastic paraplegia [54, 58, 59], Parkinson’s Disease [60, 61], Huntingdon’s Disease [62], Alzheimer’s [63], amyotrophic lateral sclerosis [64], schizophrenia [65, 66], and neuronal axonal dystrophy [67].”
A novel peptide-based strategy to enhance GBA1 expression for treating Parkinson’s disease
Kim, H., Na, J., Ryu, H. G., Lee, E., Park, H., Park, H., Nam, Y., Jeong, G., Pyo, I., Choi, J.-H., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-01175-w · Cited by 1
“At present, the precise mechanism by which hirunipin 4 enhances TFEB translocation and GCase stabilization warrants further mechanistic studies, including whether it acts via lysosomal stress signaling, mTORC1 inhibition, or direct protein – protein interactions 58 – 60 .”
Bezrukova, A. I., Basharova, K. S., Galkina, E. S., Epifanivskaya, O. S., Baydakova, G. V., Zakharova, E. Y., Pchelina, S. N., & Т.С., У. (2026) · Biomeditsinskaya Khimiya · doi:10.18097/pbmcr1616 · Cited by 1
Li, P., Wu, T., Chen, M., Wang, N., Jia, X., Chen, Z., & Duan, R. (2026) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2026.106935 · Cited by 1
Drug discovery in Alzheimer’s disease by regulating autophagy
Hamano, T., & Endo, Y. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00002-2 · Cited by 1
Damdinbazar, D., Bolortuya, B., Oyunbat, N., Ariya, E., Namuun, L., Tuvshinjargal, K., Binderiya, B., Bold, N., Davaakhuu, G., & Oyunsuren, T. (2023) · Proceedings of the Institute of Biology · doi:10.5564/pib.v39i1.3143 · Cited by 1
“During this process, enzymes act in the acidic environment of the lysosome [53].”
BackgroundDesign, synthesis, and anti-tumor activity of cyclic peptide–lenalidomide conjugated small molecules
Li, T., Li, T., Zhang, X., Xu, H., Xie, Y., Yan, R., Wu, X., Jin, Y., & Wang, Z. (2024) · New Journal of Chemistry · doi:10.1039/d3nj05320b · Cited by 1
Brijmohan, A. S. (2017) · TSpace (University of Toronto) · Cited by 1
Caracterização genótipo-fenótipo em novas síndromes associadas ao Transtorno do Espectro Autista
Branco, E. V. (2020) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.41.2020.tde-20012020-101726 · Cited by 1
CIB2 regulates autophagy via Rheb-mTORC1 signaling axisPreprint
Sethna, S., Bernstein, S. L., Jian, X., Riazuddin, S. A., Randazzo, P. A., Riazuddin, S., & Ahmed, Z. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.18.302265 · Cited by 1
Identification of TFEB gene genetic variants in acute myocardial infarctionPreprint
Zhang, J., Zhang, Y., He, X., Wang, S., Pang, S., & Yan, B. (2020) · doi:10.21203/rs.3.rs-23023/v1 · Cited by 1
Altered lipid homeostasis underlies selective neurodegeneration in SNX14 deficiencyPreprint
Zhou, Y., Sánchez, V., Xu, P. J., Flores‐Méndez, M., Ciesielski, B., Yoo, D., Teshome, H., Henne, W. M., O’Brien, T., Mesaros, C., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.30.516463 · Cited by 1
Impairment of autophagy-lysosomal activity near the chronically implanted microelectrodesPreprint
Chen, K., Padilla, C. G., Kiselyov, K. I., & Kozai, T. D. Y. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.31.543108 · Cited by 1
“TFEB is a master regulator of autophagy-lysosomal pathway, and TFEB dephosphorylation and nuclear translocation promote the expressions of genes codding for lysosomal proteins [72, 73].”
BackgroundDu, K., Chen, H., Pan, Z., Zhao, M., Cheng, S., Luo, Y., Zhang, W., & Li, D. (2025) · eLife · doi:10.7554/elife.103137.2 · Cited by 2
Insights into Glomerular Cell Biology in Health and Disease
Alghamdi, T. A. (2019) · TSpace (University of Toronto)
A Preview of Selected Articles
Atkinson, S. P. (2017) · Stem Cells Translational Medicine · doi:10.1002/sctm.17-0254
Role of Xenobiotic in Autophagy Inflection in Cell Death and Carcinogenesis
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Lifespan of Catalase-Deficient Mice Decreases Due to Lysosomal DysfunctionPreprint
Dutta, R. K., Lee, J. N., Maharjan, Y., Park, C., Choe, S., & Park, R. (2021) · Research Square · doi:10.21203/rs.3.rs-965044/v1
A Preview of Selected Articles
Atkinson, S. P. (2020) · Stem Cells · doi:10.1002/stem.3184
Lyons, D. A., & Almeida, R. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734362796.793553836
Understanding, Targeting, and Hijacking Autophagy
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The Role of Valosin-containing Protein in Organelle-specific Autophagy
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Application of Targeted Autophagy in Triple Negative Breast Cancer
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The Lysosome Signaling Platform: Adapting With the Times
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Mechanism and treatment of Alzheimer’s disease
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PAK6 promotes neuronal autophagy by regulating TFEB nuclear translocation.Preprint
Agostini, F., Agostinis, R., Rocco, M. D., Montefusco, S., Tombesi, G., Iannotta, L., Cogo, S., Lazzari, F. D., Tessari, I., Civiero, L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.05.597537
Dispensable role of mitf in melanogenesis of Xenopus tropicalis oocytesPreprint
Yi, H., Hang, J., Shen, J., Yang, S., Liu, H., Deng, J., Han, S., Feng, X., Cheng, W., Liang, W., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4807093/v1
Du, K., Chen, H., Zhao, M., Cheng, S., Luo, Y., Zhang, W., & Li, D. (2024) · eLife · doi:10.7554/elife.103137.1
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Role of autophagy‑modulating long non‑coding RNAs in tumor radioresistance (Review)
Li, H., & He, Z. (2025) · Oncology Reports · doi:10.3892/or.2025.8975
“Furthermore, the lysosomal decomposition of excess cellular parts supplies crucial raw materials and nutrients that can be reused to create important biomolecules (20).”
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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