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
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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 PD-associated genes (LRRK2, UCHL2, VCP35, DJ-1, and SNCA) affect CMA.
“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]
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× · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
A Mutation in VPS35, Encoding a Subunit of the Retromer Complex, Causes Late-Onset Parkinson Disease
Zimprich, A. 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 885 · see citing works
VPS35 Mutations in Parkinson Disease
Vilariño‐Güell, C., Wider, C. W., Ross, O. A., Dächsel, J. C., Kachergus, J. M., Lincoln, S., 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 877 · see citing works
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 850 · 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
Vogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801992200 · Cited by 683 · see citing works
Diagnosis and treatment of Parkinson disease: molecules to medicine
Savitt, J. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29178 · Cited by 649 · see citing works
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
Martínez‐Vicente, M., Tallóczy, Z., Kaushik, S., Massey, A. C., Mazzulli, J. R., Mosharov, E. V., Hodara, R., Fredenburg, R. A., Wu, D.-C., Follenzi, A., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32806 · Cited by 633 · see citing works
Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
Seaman, M. N. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200312034 · Cited by 624 · see citing works
A Role for α-Synuclein in the Regulation of Dopamine Biosynthesis
Perez, R. G., Waymire, J. C., Lin, E., Liu, J. J., Guo, F., & Zigmond, M. J. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-08-03090.2002 · Cited by 598 · see citing works
Interplay of LRRK2 with chaperone-mediated autophagy
Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588 · see citing works
Chaperone-Mediated Autophagy Markers in Parkinson Disease Brains
Alvarez‐Erviti, L., Rodríguez-Oroz, M. C., Cooper, J. A. D., Caballero, C., Ferrer, I., Obeso, J. A., & Schapira, A. H. V. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.198 · Cited by 550 · see citing works
RAB7L1 Interacts with LRRK2 to Modify Intraneuronal Protein Sorting and Parkinson’s Disease Risk
MacLeod, D. A., Rhinn, H., Kuwahara, T., Zolin, A., Paolo, G. D., McCabe, B. D., Marder, K. S., Honig, L. S., Clark, L. N., Small, S. A., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.033 · Cited by 519 · see citing works
Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1
Kamp, F., Exner, N., Lutz, A., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 505 · see citing works
Temkin, P. A., Lauffer, B. E. L., Jäger, S., Cimermančič, P., Krogan, N. J., & von Zastrow, M. (2011) · Nature Cell Biology · doi:10.1038/ncb2252 · Cited by 460 · see citing works
Bonifacino, J. S., & Hurley, J. H. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.009 · Cited by 449 · see citing works
Model‐guided microarray implicates the retromer complex in Alzheimer's disease
Small, S. A., Kent, K., Pierce, A., Leung, C., Kang, M. S., Okada, H., Honig, L., Vonsattel, J., & Kim, T. (2005) · Annals of Neurology · doi:10.1002/ana.20667 · Cited by 440 · see citing works
Villarejo, A., Burén, S., Larsson, S., Déjardin, A., Monné, M., Rudhe, C., Karlsson, J. E., Jansson, S., Lerouge, P., Rolland, N., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1330 · Cited by 369 · see citing works
Lysosomal Degradation of α-Synuclein in Vivo
Mak, S. K., McCormack, A. L., Manning-Bog, A., Cuervo, A. M., & Monte, D. A. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.074617 · Cited by 349 · see citing works
Belenkaya, T. Y., Wu, Y., Tang, X., Zhou, B., Cheng, L., Sharma, Y. V., Yan, D., Selva, E. M., & Lin, X. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.12.003 · Cited by 323 · see citing works
Recycle your receptors with retromer
Seaman, M. N. J. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.12.004 · Cited by 309 · see citing works
Alpha-synuclein and Protein Degradation Systems: a Reciprocal Relationship
Xilouri, M., Brekk, O. R., & Stefanis, L. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8341-2 · Cited by 299 · see citing works
VPS35 haploinsufficiency increases Alzheimer’s disease neuropathology
Wen, L., Tang, F., Hong, Y., Luo, S.-W., Wang, C.-L., He, W., Shen, C., Jung, J.-U., Xiong, F., Lee, D.-H., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201105109 · Cited by 264 · see citing works
Self-citationLysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity
Qiao, L., Hamamichi, S., Caldwell, K. A., Caldwell, G. A., Yacoubian, T. A., Wilson, S. M., Xie, Z., Speake, L. D., Parks, R., Crabtree, D., et al. (2008) · Molecular Brain · doi:10.1186/1756-6606-1-17 · Cited by 261 · see citing works
Wnt Signaling Requires Retromer-Dependent Recycling of MIG-14/Wntless in Wnt-Producing Cells
Yang, P., Lorenowicz, M. J., Macůrková, M., Coudreuse, D. Y. M., Betist, M. C., & Korswagen, H. C. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.12.004 · Cited by 257 · see citing works
Retromer terminates the generation of cAMP by internalized PTH receptors
Feinstein, T. N., Wehbi, V. L., Ardura, J. A., Wheeler, D., Ferrandon, S., Gardella, T. J., & Vilardaga, J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.545 · Cited by 236 · see citing works
Follett, J., Norwood, S. J., Hamilton, N., Mohan, M., Kovtun, O., Tay, S. V., Yang, Z., Wood, S. A., Mellick, G. D., Silburn, P. A., et al. (2013) · Traffic · doi:10.1111/tra.12136 · Cited by 220 · see citing works
C. elegans AP-2 and Retromer Control Wnt Signaling by Regulating MIG-14/Wntless
Pan, C., Baum, P. D., Gu, M., Jørgensen, E. M., Clark, S. G., & Garriga, G. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.12.001 · Cited by 209 · see citing works
Boosting chaperone-mediated autophagy in vivo mitigates α-synuclein-induced neurodegeneration
Xilouri, M., Brekk, O. R., Landeck, N., Pitychoutis, P. M., Papasilekas, T., Papadopoulou-Daifoti, Z., Kirik, D., & Stefanis, L. (2013) · Brain · doi:10.1093/brain/awt131 · Cited by 207 · see citing works
Miura, E., Hasegawa, T., Konno, M., Suzuki, M., Sugeno, N., Fujikake, N., Geisler, S., Tabuchi, M., Oshima, R., Kikuchi, A., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.014 · Cited by 195 · see citing works
Lin, X. Z., Parisiadou, L., Sgobio, C., Liu, G., Yu, J. H., Sun, L., Shim, H., Gu, X., Luo, J., Long, C., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1731-12.2012 · Cited by 188 · see citing works
Parkinson’s Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein
Dhungel, N., Eleuteri, S., Li, L.-B., Kramer, N. J., Chartron, J. W., Spencer, B. J., Kosberg, K. A., Fields, J. A., Stafa, K., Adame, A., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.11.027 · Cited by 176 · see citing works
SNX–BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting
van Weering, J. R. T., Verkade, P., & Cullen, P. J. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.11.009 · Cited by 171 · see citing works
Update on the genetics of Parkinson's disease
Gasser, T. (2007) · Movement Disorders · doi:10.1002/mds.21676 · Cited by 167 · see citing works
Murphy, K. E., Gysbers, A. M., Abbott, S. K., Spiro, A. S., Furuta, A., Cooper, A. A., Garner, B., Kabuta, T., & Halliday, G. M. (2015) · Movement Disorders · doi:10.1002/mds.26141 · Cited by 163 · see citing works
Tabuchi, M., Yanatori, I., Kawai, Y., & Kishi, F. (2010) · Journal of Cell Science · doi:10.1242/jcs.060574 · Cited by 143 · see citing works
Munsie, L. N., Milnerwood, A. J., Seibler, P., Beccano-Kelly, D. A., Tatarnikov, I., Khinda, J., Volta, M., Kadgien, C., Cao, L. P., Tapia, L., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu582 · Cited by 143 · see citing works
Vieira, S. I., Rebelo, S., Esselmann, H., Wiltfang, J., Lah, J. J., Lane, R. F., Small, S. A., Gandy, S., Silva, E. F. D. C. E., & Silva, O. A. B. D. C. E. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-40 · Cited by 141 · see citing works
Reversal of Behavioral Deficits and Synaptic Dysfunction in Mice Overexpressing Neuregulin 1
Yin, D., Chen, Y., Lu, Y.-S., Bean, J. C., Sathyamurthy, A., Shen, C., Liu, X., Lin, T. W., Smith, C. A., Xiong, W., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.03.028 · Cited by 139 · see citing works
Self-citationAnimal Models of Parkinson's Disease: Vertebrate GeneticsPreprint
Lee, Y., Dawson, V. L., & Dawson, T. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009324 · Cited by 129 · see citing works
Retromer Is Required for Apoptotic Cell Clearance by Phagocytic Receptor Recycling
Chen, D., Xiao, H., Zhang, K., Wang, B., Gao, Z., Jian, Y., Qi, X., Sun, J., Miao, L., & Yang, C. (2010) · Science · doi:10.1126/science.1184840 · Cited by 123 · see citing works
Phosphatidylinositol transfer protein-α in netrin-1-induced PLC signalling and neurite outgrowth
Xie, Y., Ding, Y., Hong, Y., Zhu, F., Navarre, S., Xi, C.-X., Zhu, X., Wang, C.-L., Ackerman, S. L., Kozlowski, D. J., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1321 · Cited by 120 · see citing works
Self-citationMcFarland, N. R., Lee, J., Hyman, B. T., & McLean, P. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06010.x · Cited by 91 · see citing works
von Coelln, R., Thomas, B., Andrabi, S. A., Lim, K. L., Savitt, J. M., Saffary, R., Stirling, W. L. H., Bruno, K. J., Hess, E. J., Lee, M. K., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0414-06.2006 · Cited by 90 · see citing works
Mitochondrial Dynamics and Parkinson's Disease: Focus on Parkin
Lim, K., Ng, X., Grace, L. G.-Y., & Yao, T. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4105 · Cited by 79 · see citing works
Wang, C.-L., Tang, F., Peng, Y. W., Shen, C.-Y., Mei, L., & Xiong, W. (2012) · Biology Open · doi:10.1242/bio.20122451 · Cited by 75 · see citing works
Self-citationMalkus, K. A., & Ischiropoulos, H. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.017 · Cited by 71 · see citing works
Huang, X., Hartley, A.-V., Yin, Y., Herskowitz, J. H., Lah, J. J., & Ressler, K. J. (2013) · Journal of Virological Methods · doi:10.1016/j.jviromet.2013.06.008 · Cited by 68 · see citing works
Xia, W.-F., Tang, F.-L., Xiong, L., Xiong, S., Jung, J.-U., Lee, D., Li, X.-S., Feng, X., Mei, L., & Xiong, W.-C. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201207154 · Cited by 48 · see citing works
Self-citationLive imaging of synaptic vesicle release and retrieval in dopaminergic neurons
Mani, M. (2009) · Frontiers in Neural Circuits · doi:10.3389/neuro.04.003.2009 · Cited by 45 · see citing works
Liu, W., Tang, F., Erion, J., Xiao, H., Ye, J., & Xiong, W. (2014) · Molecular Brain · doi:10.1186/1756-6606-7-10 · Cited by 23 · see citing works
Self-citation
Flagged first, then by citations
1 of the 55 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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 · see citing works
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 1,422 · see citing works
Mitochondrial dysfunction in Parkinson's disease
Bose, A., & Beal, M. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13731 · Cited by 598 · see citing works
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 594 · see citing works
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 · see citing works
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 485 · see citing works
Defects in trafficking bridge Parkinson’s disease pathology and genetics
Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462 · see citing works
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 382 · see citing works
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 355 · see citing works
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 · see citing works
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 274 · see citing works
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 266 · see citing works
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 255 · see citing works
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 238 · see citing works
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 · see citing works
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 194 · see citing works
Alpha-Synuclein Physiology and Pathology: A Perspective on Cellular Structures and Organelles
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 188 · see citing works
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 179 · see citing works
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 180 · see citing works
VPS35, the Retromer Complex and Parkinson’s Disease
Williams, E. T., Chen, X., & Moore, D. J. (2017) · Journal of Parkinson s Disease · doi:10.3233/jpd-161020 · Cited by 173 · see citing works
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 165 · see citing works
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 164 · see citing works
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 · see citing works
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 153 · see citing works
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 145 · see citing works
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 · 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
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 138 · see citing works
Role of the endolysosomal system in Parkinson’s disease
Vidyadhara, D. J., Lee, J. E., & Chandra, S. S. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14820 · Cited by 131 · see citing works
Autophagy lysosomal pathway dysfunction in Parkinson's disease; evidence from human genetics
Senkevich, K. A., & Gan‐Or, Z. (2019) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2019.11.015 · Cited by 135 · see citing works
The Prion-Like Spreading of Alpha-Synuclein in Parkinson’s Disease: Update on Models and Hypotheses
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 126 · see citing works
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 · see citing works
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 · see citing works
The Vicious Cycle Between α ‐Synuclein Aggregation and Autophagic‐Lysosomal Dysfunction
Bellomo, G., Paciotti, S., Gatticchi, L., & Parnetti, L. (2019) · Movement Disorders · doi:10.1002/mds.27895 · Cited by 114 · see citing works
Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases
Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111 · see citing works
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 · see citing works
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 108 · see citing works
The Multiple Roles of Autophagy in Neural Function and Diseases
Li, Y., Qin, Z., & Sheng, R. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01120-y · Cited by 106 · see citing works
Endosomal sorting and trafficking, the retromer complex and neurodegeneration
Vagnozzi, A. N., & Praticò, D. (2018) · Molecular Psychiatry · doi:10.1038/s41380-018-0221-3 · Cited by 95 · see citing works
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 102 · see citing works
Glucocerebrosidase and Parkinson Disease: Molecular, Clinical, and Therapeutic Implications
Balestrino, R., & Schapira, A. H. V. (2018) · The Neuroscientist · doi:10.1177/1073858417748875 · Cited by 96 · see citing works
Wise, R. M., Wagener, A., Fietzek, U. M., Klopstock, T., Mosharov, E. V., Zucca, F. A., Sulzer, D. L., Zecca, L., & Burbulla, L. F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105920 · Cited by 95 · see citing works
The Retromer Complex and Sorting Nexins in Neurodegenerative Diseases
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 89 · see citing works
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 84 · see citing works
ɑ‐Synuclein strains and the variable pathologies of synucleinopathies
Peelaerts, W., & Baekelandt, V. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13595 · Cited by 89 · see citing works
α-Synuclein-carrying extracellular vesicles in Parkinson’s disease: deadly transmitters
Chistiakov, D. A., & Chistiakov, A. A. (2016) · Acta Neurologica Belgica · doi:10.1007/s13760-016-0679-1 · Cited by 86 · see citing works
Quantitative proteomic analysis of Parkin substrates in Drosophila neurons
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 83 · see citing works
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 82 · see citing works
Self-citationTian, Y., Tang, F., Sun, X.-D., Wen, L., Mei, L., Tang, B.-S., & Xiong, W. (2015) · Molecular Brain · doi:10.1186/s13041-015-0156-4 · Cited by 82 · see citing works
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 79 · see citing works
Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79 · see citing works
Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease
Pitcairn, C., Wani, W. Y., & Mazzulli, J. R. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.03.008 · Cited by 75 · see citing works
Autophagy in Astrocytes and its Implications in Neurodegeneration
Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 74 · see citing works
Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson’s Disease
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 76 · see citing works
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 68 · see citing works
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 67 · see citing works
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 64 · see citing works
Rani, L., & Mondal, A. C. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.09.010 · Cited by 68 · see citing works
The Emerging Roles of Autophagy in Human Diseases
Lei, Y., & Klionsky, D. J. (2021) · Biomedicines · doi:10.3390/biomedicines9111651 · Cited by 66 · see citing works
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 62 · see citing works
Are rodent models of Parkinson’s disease behaving as they should?
Vingill, S., Connor‐Robson, N., & Wade‐Martins, R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.10.021 · Cited by 60 · see citing works
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 61 · see citing works
Wang, Y.-T., & Lu, J. (2022) · Cells · doi:10.3390/cells11142250 · Cited by 60 · see citing works
The LRRK2–macroautophagy axis and its relevance to Parkinson's disease
Manzoni, C. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160265 · Cited by 57 · see citing works
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 60 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Peña‐Díaz, S., García‐Pardo, J., & Ventura, S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030839 · Cited by 53 · see citing works
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 52 · see citing works
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 · see citing works
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 50 · see citing works
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 51 · see citing works
Limanaqi, F., Biagioni, F., Gambardella, S., Ryskalin, L., & Fornai, F. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00299 · Cited by 49 · see citing works
Ye, H., Ojelade, S. A., Li‐Kroeger, D., Zuo, Z., Wang, L., Li, Y., Gu, J. Y. J., Tepaß, U., Rodal, A. A., Bellen, H. J., et al. (2020) · eLife · doi:10.7554/elife.51977 · Cited by 52 · see citing works
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 · see citing works
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 49 · see citing works
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 50 · see citing works
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 · see citing works
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 49 · see citing works
Tang, F., Zhao, L., Zhao, Y., Sun, D., Zhu, X., Mei, L., & Xiong, W. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-019-0487-2 · Cited by 47 · see citing works
Self-citationCourtland, J. L., Bradshaw, T. W., Waitt, G. M., Soderblom, E. J., Ho, T., Rajab, A., Vancini, R. G., Kim, H., & Soderling, S. H. (2021) · eLife · doi:10.7554/elife.61590 · Cited by 46 · see citing works
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 46 · see citing works
VPS35 D620N knockin mice recapitulate cardinal features of Parkinson’s disease
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 · see citing works
Ren, X., Yao, L., Wang, Y., Mei, L., & Xiong, W. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02422-0 · Cited by 44 · see citing works
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 46 · see citing works
Hu, D., Liu, Z., & Qi, X. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.746873 · Cited by 44 · see citing works
Wang, W., Ma, X., Zhou, L., Liu, J., & Zhu, X. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw430 · Cited by 44 · see citing works
Impact of Chaperone-Mediated Autophagy in Brain Aging: Neurodegenerative Diseases and Glioblastoma
Auzmendi-Iriarte, J., & Matheu, A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.630743 · Cited by 45 · see citing works
Alpha-Synuclein and the Endolysosomal System in Parkinson’s Disease: Guilty by Association
Teixeira, M., Sheta, R., Idi, W., & Oueslati, A. (2021) · Biomolecules · doi:10.3390/biom11091333 · Cited by 43 · see citing works
Daly, J. L., Danson, C. M., Lewis, P. A., Zhao, L., Riccardo, S., Filippo, L. D., Cacchiarelli, D., Lee, D., Cross, S., Heesom, K. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38719-8 · Cited by 41 · see citing works
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 42 · see citing works
VPS35 and the mitochondria: Connecting the dots in Parkinson's disease pathophysiology
Cutillo, G., Simon, D. K., & Eleuteri, S. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105056 · Cited by 42 · see citing works
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 41 · see citing works
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 37 · see citing works
Ghrelin mediated neuroprotection - A possible therapy for Parkinson's disease?
Morgan, A., Rees, D., Andrews, Z., & Davies, J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.12.027 · Cited by 39 · see citing works
Kato, K., Oka, Y., Muramatsu, H., Vasilyev, F. F., Otomo, T., Oishi, H., Kawano, Y., Kidokoro, H., Nakazawa, Y., Ogi, T., et al. (2019) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2019-106213 · Cited by 39 · see citing works
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 38 · see citing works
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 · see citing works
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 · see citing works
- 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 › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › 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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