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VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for -Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease
Open accessAbstract
Vacuolar protein sorting-35 (VPS35) is essential for endosome-to-Golgi retrieval of membrane proteins. Mutations in the VPS35 gene have been identified in patients with autosomal dominant PD. However, it remains poorly understood if and how VPS35 deficiency or mutation contributes to PD pathogenesis. Here we provide evidence that links VPS35 deficiency to PD-like neuropathology. VPS35 was expressed in mouse dopamine (DA) neurons in substantia nigra pars compacta (SNpc) and STR (striatum)--regions that are PD vulnerable. VPS35-deficient mice exhibited PD-relevant deficits including accumulation of α-synuclein in SNpc-DA neurons, loss of DA transmitter and DA neurons in SNpc and STR, and impairment of locomotor behavior. Further mechanical studies showed that VPS35-deficient DA neurons or DA neurons expressing PD-linked VPS35 mutant (D620N) had impaired endosome-to-Golgi retrieval of lysosome-associated membrane glycoprotein 2a (Lamp2a) and accelerated Lamp2a degradation. Expression of Lamp2a in VPS35-deficient DA neurons reduced α-synuclein, supporting the view for Lamp2a as a receptor of chaperone-mediated autophagy to be critical for α-synuclein degradation. These results suggest that VPS35 deficiency or mutation promotes PD pathogenesis and reveals a crucial pathway, VPS35-Lamp2a-α-synuclein, to prevent PD pathogenesis. Significance statement: VPS35 is a key component of the retromer complex that is essential for endosome-to-Golgi retrieval of membrane proteins. Mutations i…
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“At least five other genes that are associated with PD (but not LSDs) also affect CMA: LRRK2, UCHL2, VCP35, DJ-1, and SNCA, which encodes alpha-synuclein.149–153”
From The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases (2025) · cites this paper as [152]
In the citing paper
“VPS35 deficiency alters the distribution of lysosome-associated membrane glycoprotein 2a (Lamp2a) in neurons19.”
From Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis (2020) · cites this paper as [19]
Citations
Cites
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · cited 1×
“This view is in agreement with reports that -synuclein mutant identified in PD patients impairs its degradation, resulting in its accumulation (Cuervo et al., 2004), and overexpression of WT -synuclein is sufficient to cause a PD-like deficit in mice (Lin et al., 2012).”
Resultα-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
Yoshimori, T., Yamamoto, A., Moriyama, Y., Futai, M., & Tashiro, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47429-2 · Cited by 1,334
The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease
Rogaeva, E., Meng, Y., Lee, J. H., Gu, Y., Kawarai, T., Zou, F., Katayama, T., Baldwin, C. T., Cheng, R., Hasegawa, H., et al. (2007) · Nature Genetics · doi:10.1038/ng1943 · Cited by 1,167
Chaperone-mediated autophagy: roles in disease and aging
Cuervo, A. M., & Wong, E. S. P. (2013) · Cell Research · doi:10.1038/cr.2013.153 · Cited by 899
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 · cited 1×
“…pathogenesis, multiple cellular deficits are induced by overexpression of -synuclein in DA neurons, including impairment of DA transmitter release (Perez et al., 2002), mitochondrial fission deficit (Kamp et al., 2010; Lim et al., 2012), and altered autophagosome formation (Winslow et al., 2010).”
BackgroundA Mutation in VPS35, Encoding a Subunit of the Retromer Complex, Causes Late-Onset Parkinson Disease
Zimprich, A., Benet-Pagès, A., Struhal, W., Graf, E., Eck, S. H., Offman, M. N., Haubenberger, D., Spielberger, S., Schulte, E. C., Lichtner, P., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.008 · Cited by 816
VPS35 mutations in Parkinson disease
Vilariño-Güell, C., Wider, C., Ross, O. A., Dachsel, J. C., Kachergus, J. M., Lincoln, S. J., Soto-Ortolaza, A. I., Cobb, S. A., Wilhoite, G. J., Bacon, J. A., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.001 · Cited by 800
Vogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801992200 · Cited by 683
Diagnosis and treatment of Parkinson disease: molecules to medicine
Savitt, J. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29178 · Cited by 660
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Poewe, W., Seppi, K., Tanner, C. M., Halliday, G. M., Brundin, P., Volkmann, J., Schrag, A.-E., & Lang, A. E. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.13 · Cited by 5,415
The coming of age of chaperone-mediated autophagy
Kaushik, S., & Cuervo, A. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0001-6 · Cited by 1,407
Mitochondrial dysfunction in Parkinson's disease
Bose, A., & Beal, M. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13731 · Cited by 915
Understanding Dopaminergic Cell Death Pathways in Parkinson Disease
Michel, P. P., Hirsch, É. C., & Hunot, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.038 · Cited by 622
To degrade or not to degrade: Mechanisms and significance of endocytic recycling
Cullen, P. J., & Steinberg, F. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0053-7 · Cited by 590
The different autophagy degradation pathways and neurodegeneration
Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 500
Defects in trafficking bridge Parkinson’s disease pathology and genetics
Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462
Mazzulli, J. R., Zunke, F., Ole Isacson, A., Studer, L., & Krainc, D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520335113 · Cited by 398
Autophagy in Parkinson's Disease
Hou, X., Watzlawik, J. O., Fiesel, F. C., & Springer, W. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.037 · Cited by 361
Selective 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
Tang, F., Liu, W., Hu, J.-X., Erion, J., Ye, J., Mei, L., & Xiong, W. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.08.001 · Cited by 283
Self-citationAutophagy and A lpha‐ S ynuclein: R elevance to P arkinson's D isease and R elated S ynucleopathies
Xilouri, M., Brekk, O. R., & Stefanis, L. (2016) · Movement Disorders · doi:10.1002/mds.26477 · Cited by 280
Autophagy, aging, and age-related neurodegeneration
Palmer, J. E., Wilson, N., Son, S. M., Obrocki, P., Wróbel, L., Rob, M., Takla, M., Korolchuk, V. I., & Rubinsztein, D. C. (2024) · Neuron · doi:10.1016/j.neuron.2024.09.015 · Cited by 277
Autophagy 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 244
Impaired dopamine release in Parkinson’s disease
Cramb, K. M. L., Beccano-Kelly, D., Cragg, S. J., & Wade-Martins, R. (2023) · Brain · doi:10.1093/brain/awad064 · Cited by 207
Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease
Zeng, X., Geng, W.-S., Jia, J., Chen, L., & Zhang, P.-P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00109 · Cited by 203
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Bernal-Conde, L. D., Ramos-Acevedo, R., Reyes-Hernández, M. A., Balbuena-Olvera, A. J., Morales-Moreno, I. D., Argüero‐Sánchez, R., Schüle, B., & Guerra‐Crespo, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01399 · Cited by 197
GBA1 deficiency negatively affects physiological α-synuclein tetramers and related multimers
Kim, S., Yun, S. P., Lee, S., Umanah, G. K. E., Bandaru, V. V. R., Yin, X., Rhee, P., Karuppagounder, S. S., Kwon, S., Lee, H., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1700465115 · Cited by 180
Mitochondrial dynamics in Parkinson's disease: a role for α-synuclein?
Devoto, V. M. P., & Falzone, T. L. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.026294 · Cited by 184
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Williams, E. T., Chen, X., & Moore, D. J. (2017) · Journal of Parkinson s Disease · doi:10.3233/jpd-161020 · Cited by 178
Karpowicz, R. J., Haney, C. M., Mihaila, T. S., Frasier, R. M., Petersson, E. J., & Lee, V. M. ‐. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.780296 · Cited by 173
The cell biology of Parkinson’s disease
Panicker, N., Ge, P., Dawson, V. L., & Dawson, T. M. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202012095 · Cited by 179
Kuo, S.-H., Tasset, I., Cheng, M. M., Diaz, A., Pan, M.-K., Lieberman, O. J., Hutten, S. J., Alcalay, R. N., Kim, S., Ximénez-Embún, P., et al. (2022) · Science Advances · doi:10.1126/sciadv.abm6393 · Cited by 153
Endocytic membrane trafficking and neurodegenerative disease
Schreij, A. M. A., Fon, E. A., & McPherson, P. S. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2105-x · Cited by 160
Dysfunction of Cellular Proteostasis in Parkinson’s Disease
Lehtonen, Š., Sonninen, T.-M., Wojciechowski, S., Goldsteins, G., & Koıstınaho, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00457 · Cited by 152
Quadri, M., Mandemakers, W., Grochowska, M. M., Masius, R., Geut, H., Fabrizio, E., Breedveld, G. J., Kuipers, D., Minneboo, M., Vergouw, L. J. M., et al. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30179-0 · Cited by 143
Autophagy impairment in Parkinson’s disease
Karabiyik, C., Lee, M. J., & Rubinsztein, D. C. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170023 · Cited by 141
DJ-1 Inhibits α-Synuclein Aggregation by Regulating Chaperone-Mediated Autophagy
Xu, C., Kang, W., Chen, Y., Jiang, T., Zhang, J., Zhang, L., Ding, J., Liu, J., & Chen, S. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00308 · Cited by 143
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Vidyadhara, D. J., Lee, J. E., & Chandra, S. S. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14820 · Cited by 137
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Senkevich, K. A., & Gan‐Or, Z. (2019) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2019.11.015 · Cited by 138
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Jan, A., Gonçalves, N. P., Vægter, C. B., Jensen, P. H., & Ferreira, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158338 · Cited by 133
ER stress and Parkinson's disease: Pathological inputs that converge into the secretory pathway
Mercado, G., Castillo, V., Soto, P., & Sidhu, A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.042 · Cited by 119
Chen, X., Kordich, J. K., Williams, E. T., Levine, N. D., Cole-Strauss, A., Marshall, L. L., Labrie, V., Ma, J., Lipton, J. W., & Moore, D. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814909116 · Cited by 114
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Bellomo, G., Paciotti, S., Gatticchi, L., & Parnetti, L. (2019) · Movement Disorders · doi:10.1002/mds.27895 · Cited by 116
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Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111
Ren, Z., Wang, C., Wang, T., Ding, H., Zhou, M., Yang, N., Liu, Y., & Chan, P. (2018) · Acta Pharmacologica Sinica · doi:10.1038/s41401-018-0077-8 · Cited by 109
Wang, Z., Liu, J., Zhu, Z., Su, C.-F., Sreenivasmurthy, S. G., Iyaswamy, A., Lu, J., Chen, G., Song, J., & Li, M. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110968 · Cited by 109
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Li, Y., Qin, Z., & Sheng, R. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01120-y · Cited by 109
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Vagnozzi, A. N., & Praticò, D. (2019) · Molecular Psychiatry · doi:10.1038/s41380-018-0221-3 · Cited by 95
Key genes and convergent pathogenic mechanisms in Parkinson disease
Coukos, R., & Krainc, D. (2024) · Nature reviews. Neuroscience · doi:10.1038/s41583-024-00812-2 · Cited by 116
Glucocerebrosidase and Parkinson Disease: Molecular, Clinical, and Therapeutic Implications
Balestrino, R., & Schapira, A. H. V. (2018) · The Neuroscientist · doi:10.1177/1073858417748875 · Cited by 105
Wise, R. M., Wagener, A., Fietzek, U. M., Klopstock, T., Mosharov, E. V., Zucca, F. A., Sulzer, D., Zecca, L., & Burbulla, L. F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105920 · Cited by 96
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Zhang, H., Huang, T. Y., Hong, Y., Yang, W., Zhang, X., Luo, H., Xu, H., & Wang, X. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00079 · Cited by 92
LRRK2 and α-Synuclein: Distinct or Synergistic Players in Parkinson’s Disease?
O’Hara, D. M., Pawar, G. N., Kalia, S. K., & Kalia, L. V. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00577 · Cited by 89
ɑ‐Synuclein strains and the variable pathologies of synucleinopathies
Peelaerts, W., & Baekelandt, V. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13595 · Cited by 96
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Chistiakov, D. A., & Chistiakov, A. A. (2016) · Acta Neurologica Belgica · doi:10.1007/s13760-016-0679-1 · Cited by 87
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Martinez, A., Lectez, B. L. P., Ramírez, J., Popp, O., Sutherland, J. D., Urbé, S., Dittmar, G., Clague, M. J., & Mayor, U. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0170-3 · Cited by 86
Appel, J. R., Ye, S., Tang, F., Sun, D., Zhang, H., Mei, L., & Xiong, W. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.3621-17.2018 · Cited by 86
Self-citationTian, Y., Tang, F.-L., Sun, X., Wen, L., Mei, L., Tang, B.-S., & Xiong, W.-C. (2015) · Molecular Brain · doi:10.1186/s13041-015-0156-4 · Cited by 76
Self-citationα-synuclein impairs autophagosome maturation through abnormal actin stabilization
Sarkar, S., Olsen, A. L., Sygnecka, K., Lohr, K. M., & Feany, M. Β. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009359 · Cited by 82
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Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79
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Pitcairn, C., Wani, W. Y., & Mazzulli, J. R. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.03.008 · Cited by 75
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Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 78
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Saramowicz, K., Siwecka, N., Galita, G., Kucharska-Lusina, A., Rozpędek‐Kamińska, W., & Majsterek, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010360 · Cited by 79
Impaired striatal dopamine release in homozygous Vps35 D620N knock-in mice
Ishizu, N., Yui, D., Hebisawa, A., Aizawa, H., Cui, W., Fujita, Y., Hashimoto, K., Ajioka, I., Mizusawa, H., Yokota, T., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw279 · Cited by 71
The Role of VPS35 in the Pathobiology of Parkinson’s Disease
Sassone, J., Reale, C., Dati, G., Regoni, M., Pellecchia, M. T., & Garavaglia, B. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00849-8 · Cited by 72
Rani, L., & Mondal, A. C. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.09.010 · Cited by 68
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Lei, Y., & Klionsky, D. J. (2021) · Biomedicines · doi:10.3390/biomedicines9111651 · Cited by 68
Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis
Muzio, L., Sirtori, R., Gornati, D., Eleuteri, S., Fossaghi, A., Brancaccio, D., Manzoni, L., Ottoboni, L., Feo, L. D., Quattrini, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17524-7 · Cited by 65
Chaperone mediated autophagy in aging: Starve to prosper
Xilouri, M., & Stefanis, L. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.001 · Cited by 65
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Vingill, S., Connor‐Robson, N., & Wade‐Martins, R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.10.021 · Cited by 63
Koprich, J. B., Johnston, T. H., Reyes, G., Omana, V. N., & Brotchie, J. M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167235 · Cited by 64
Wang, Y.-T., & Lu, J. (2022) · Cells · doi:10.3390/cells11142250 · Cited by 62
The LRRK2–macroautophagy axis and its relevance to Parkinson's disease
Manzoni, C. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160265 · Cited by 57
The emerging role of retromer in neuroprotection
McMillan, K. J., Korswagen, H. C., & Cullen, P. J. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.004 · Cited by 66
Deregulation of autophagy and vesicle trafficking in Parkinson’s disease
Sheehan, P., & Yue, Z. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.013 · Cited by 56
Mitochondrial and Clearance Impairment in p. D620N VPS35 Patient‐Derived Neurons
Hanss, Z., Larsen, S. B., Antony, P. M. A., Mencke, P., Massart, F., Jarazo, J., Schwamborn, J. C., Barbuti, P. A., Mellick, G. D., & Krüger, R. (2020) · Movement Disorders · doi:10.1002/mds.28365 · Cited by 57
Chen, Z., Nie, S., Qu, M., Zhou, D., Wu, L., Shi, X., Ma, L.-R., Li, X., Zhou, S., Wang, S., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0795-3 · Cited by 55
Peña‐Díaz, S., García‐Pardo, J., & Ventura, S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030839 · Cited by 54
VPS35 regulates cell surface recycling and signaling of dopamine receptor D1
Wang, C., Niu, M., Zhou, Z., Zheng, X., Zhang, L., Tian, Y., Yu, X., Bu, G., Xu, H., Ma, Q., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.05.016 · Cited by 55
Self-citationKim, M. J., Deng, H., Wong, Y. C., Siddique, T., & Krainc, D. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw413 · Cited by 52
Contributions of VPS35 Mutations to Parkinson’s Disease
Rahman, A. A., & Morrison, B. E. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.01.006 · Cited by 55
Lysosomal dysfunction in α-synuclein pathology: molecular mechanisms and therapeutic strategies
Dai, L., Liu, M., Ke, W., Chen, L., Fang, X., & Zhang, Z. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05419-5 · Cited by 53
Limanaqi, F., Biagioni, F., Gambardella, S., Ryskalin, L., & Fornai, F. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00299 · Cited by 50
Ye, H., Ojelade, S. A., Li-Kroeger, D., Zuo, Z., Wang, L., Li, Y., Gu, J. Y., Tepass, U., Rodal, A. A., Bellen, H. J., et al. (2020) · eLife · doi:10.7554/elife.51977 · Cited by 51
Chiu, C., Weng, Y.-H., Huang, Y., Chen, R., Liu, Y., Yeh, T., Lu, C., Lin, Y., Chen, Y.-J., Hsu, C., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03228-9 · Cited by 51
Understanding the contributions of VPS35 and the retromer in neurodegenerative disease
Williams, E. T., Chen, X., Otero, P. A., & Moore, D. J. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105768 · Cited by 51
Modulating Chaperone-Mediated Autophagy and Its Clinical Applications in Cancer
Hubert, V., Weiss, S., Rees, A. J., & Kain, R. (2022) · Cells · doi:10.3390/cells11162562 · Cited by 51
Parkinson's disease-associated pathogenic VPS35 mutation causes complex I deficits
Zhou, L., Wang, W., Hoppel, C. L., Liu, J., & Zhu, X. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.07.032 · Cited by 49
Nie, T., Tao, K., Zhu, L., Huang, L. H., Hu, S., Yang, R., Xu, P., Mao, Z., & Yang, Q. (2020) · Autophagy · doi:10.1080/15548627.2020.1848128 · Cited by 51
Tang, F.-L., Zhao, L., Zhao, Y., Sun, D., Zhu, X.-J., Mei, L., & Xiong, W.-C. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0487-2 · Cited by 47
Self-citationCourtland, J. L., Bradshaw, T. W., Waitt, G., Soderblom, E. J., Ho, T., Rajab, A., Vancini, R., Kim, I. H., & Soderling, S. H. (2021) · eLife · doi:10.7554/elife.61590 · Cited by 49
Advances in animal models of Parkinson's disease
He, S., Ru, Q., Chen, L., Xu, G., & Wu, Y. (2024) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2024.111024 · Cited by 54
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Niu, M., Zhao, F., Bondelid, K. S., Siedlak, S. L., Torres, S. L., Fujioka, H., Wang, W., Liu, J., & Zhu, X. (2021) · Aging Cell · doi:10.1111/acel.13347 · Cited by 46
Ren, X., Yao, L., Wang, Y., Mei, L., & Xiong, W.-C. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02422-0 · Cited by 42
Self-citationBoon, N., Lu, X., Andriessen, C. A., Moustakas, I., Buck, T. M., Freund, C., Arendzen, C. H., Böhringer, S., Boon, C. J. F., Mei, H., et al. (2023) · Stem Cell Reports · doi:10.1016/j.stemcr.2023.03.014 · Cited by 49
Hu, D., Liu, Z., & Qi, X. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.746873 · Cited by 44
Wang, W., Ma, X., Zhou, L., Liu, J., & Zhu, X. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw430 · Cited by 45
Impact of Chaperone-Mediated Autophagy in Brain Aging: Neurodegenerative Diseases and Glioblastoma
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Daly, J. L., Danson, C. M., Lewis, P. A., Zhao, L., Riccardo, S., Di Filippo, L., Cacchiarelli, D., Lee, D., Cross, S. J., Heesom, K. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38719-8 · Cited by 45
Self-citationEndolysosomal dysfunction in Parkinson's disease: Recent developments and future challenges
Kett, L. R., & Dauer, W. T. (2016) · Movement Disorders · doi:10.1002/mds.26797 · Cited by 43
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Cutillo, G., Simon, D. K., & Eleuteri, S. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105056 · Cited by 43
Exploring the Role of Autophagy Dysfunction in Neurodegenerative Disorders
Rana, T., Behl, T., Sehgal, A., Mehta, V., Singh, S., Bhatia, S., Al‐Harrasi, A., & BUNGAU, S. G. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02472-0 · Cited by 42
Mishra, J., Bhatti, G. K., Sehrawat, A., Singh, C., Singh, A., Reddy, A. P., Reddy, P. H., & Bhatti, J. S. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121153 · Cited by 38
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Morgan, A. H., Rees, D. J., Andrews, Z. B., & Davies, J. S. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.12.027 · Cited by 40
Kato, K., Oka, Y., Muramatsu, H., Vasilev, F. F., Otomo, T., Oishi, H., Kawano, Y., Kidokoro, H., Nakazawa, Y., Ogi, T., et al. (2020) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2019-106213 · Cited by 42
Chaperone-mediated autophagy as a therapeutic target for Parkinson disease
Campbell, P., Morris, H. R., & Schapira, A. H. V. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1517156 · Cited by 39
Mohan, A. G., Calenic, B., Ghiurau, N. A., Duncea-Borca, R., Constantinescu, A.-E., & Constantinescu, I. (2023) · Cells · doi:10.3390/cells12151972 · Cited by 36
Chaperone-mediated autophagy: Advances from bench to bedside
Li, W., Nie, T., Xu, H., Yang, J. H., Yang, Q., & Mao, Z. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.010 · Cited by 36
Metadata
- Authors
- Tang, F.-L., Erion, J. R., Tian, Y., Liu, W., Yin, D.-M., Ye, J., Tang, B., Mei, L., & Xiong, W.-C.
- Affiliations
- Augusta University (US)
- Central South University (CN)
- Army Medical University (CN)
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2015-07-22
- Volume
- 35
- Issue
- 29
- Pages
- 10613-10628
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC4510296
- OpenAlex
- W1953962861
- Cited by
- 269
- References
- 55
- Citations by year
- 2026: 14 · 2025: 10 · 2024: 28 · 2023: 28 · 2022: 19 · 2021: 34 · 2020: 39 · 2019: 19 · 2018: 26 · 2017: 22 · 2016: 26 · 2015: 4
- Type
- conference abstract
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Neuroscience (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01 BX000838)
- National Institutes of Health (AG045781)
- National Institute on Aging (R01AG045781, RF1AG045781, AG045781)
- National Institute of Neurological Disorders and Stroke (P30NS055077)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- VPS35, Parkinson's disease, dopaminergic neurons, LAMP2A, chaperone-mediated autophagy, alpha-synuclein degradation, retromer complex, substantia nigra pars compacta, striatum
- MeSH terms
- Animals, Autophagy, Cells, Cultured, Golgi Apparatus, Mice, Inbred C57BL, Mice, Mutant Strains, Endosomes, Transfection, Blotting, Western, Mutagenesis, Site-Directed, Microscopy, Confocal, Parkinsonian Disorders, Protein Transport, Vesicular Transport Proteins, Mice, alpha-Synuclein, Lysosomal-Associated Membrane Protein 2, Dopaminergic Neurons, Real-Time Polymerase Chain Reaction
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