Autophagy activation and enhanced mitophagy characterize the Purkinje cells of pcd mice prior to neuronal death
Open accessAbstract
Purkinje cells are a class of specialized neurons in the cerebellum, and are among the most metabolically active of all neurons, as they receive immense synaptic stimulation, and provide the only efferent output from the cerebellum. Degeneration of Purkinje cells is a common feature of inherited ataxias in humans and mice. To understand Purkinje neuron degeneration, investigators have turned to naturally occurring Purkinje cell degeneration phenotypes in mice to identify key regulatory proteins and cellular pathways. The Purkinje cell degeneration (pcd) mouse is a recessive mutant characterized by complete and dramatic post-natal, cell autonomous Purkinje neuron degeneration and death. As the basis of Purkinje cell death in pcd is unresolved, and contradictory data has emerged for the role of autophagy in Purkinje cell degeneration, we studied the mechanism of Purkinje cell death in pcd mice. BAX null status did not suppress Purkinje neuron death in pcd mice, indicating that classic apoptosis is not responsible for Purkinje cell loss. Interestingly, LC3 Western blot analysis and GFP-LC3 immunostaining of degenerating pcd cerebellum revealed activation of the autophagy pathway. Ultrastructural studies confirmed increased autophagy pathway activity in Purkinje cells, and yielded evidence for mitophagy, in agreement with LC3 immunoblotting of cerebellar fractions. As p62 levels were decreased in pcd cerebellum, our findings suggest that pcd Purkinje cell neurons can execute effective autophagy. However, our results support a role for dysregulated autophagy activation in pcd, and suggest that increased or aberrant mitophagy contributes to the Purkinje cell degeneration in pcd mice.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Purkinje cell degeneration models such as pcd mice display motor abnormalities that were similar to those observed in B6.Clec16aGT/GT and Clec16aCURT/CURT mice.
“Purkinje cell degeneration models such as pcd mice display motor abnormalities that were similar to those observed in B6.Clec16aGT/GT and Clec16aCURT/CURT mice3031 and staining with the Purkinje cell marker calbindin confirmed loss of these cells in B6.Clec16aGT/GT mice (Fig. 2d) at 8 weeks of age that was dramatically increased by 47 weeks of age (Supplementary Fig. 2e).”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [30]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069 · see citing works
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605 · see citing works
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882 · see citing works
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · see citing works
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,532 · see citing works
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,323 · see citing works
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588 · see citing works
Selective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558 · see citing works
Regulation of an ATG7 - beclin 1 Program of Autophagic Cell Death by Caspase-8
Yu, L., Alva, A. S., Su, H. C., Dutt, P., Freundt, E. C., Welsh, S. J., Baehrecke, E. H., & Lenardo, M. J. (2004) · Science · doi:10.1126/science.1096645 · Cited by 1,220 · see citing works
Autophagy: dual roles in life and death?
Baehrecke, E. H. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1666 · Cited by 986 · see citing works
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967 · see citing works
Dagda, R. K., Cherra, S. J., Kulich, S. M., Tandon, A., Park, D., & Chu, C. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808515200 · Cited by 954 · see citing works
Methods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656 · see citing works
Komatsu, M., Wang, Q. J., Holstein, G. R., Friedrich, V. L., Iwata, J.-I., Kominami, E., Chait, B. T., Tanaka, K., & Yue, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701311104 · Cited by 614 · see citing works
Purkinje cell degeneration, a new neurological mutation in the mouse.
Mullen, R. J., Eicher, E. M., & Sidman, R. L. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.1.208 · Cited by 611 · see citing works
Neurodegeneration in Lurcher mice caused by mutation in δ2 glutamate receptor gene
Zuo, J., De Jager, P. L., Takahashi, K. A., Jiang, W., Linden, D. J., & Heintz, N. (1997) · Nature · doi:10.1038/42009 · Cited by 554 · see citing works
Widespread Elimination of Naturally Occurring Neuronal Death inBax-Deficient Mice
White, F. A., Keller-Peck, C. R., Knudson, C. M., Korsmeyer, S. J., & Snider, W. D. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-04-01428.1998 · Cited by 436 · see citing works
Autophagy in neurodegenerative disease: friend, foe or turncoat?
Nixon, R. A. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.07.003 · Cited by 315 · see citing works
A Novel Protein Complex Linking the δ2 Glutamate Receptor and Autophagy
Yue, Z., Horton, A., Bravin, M., DeJager, P. L., Selimi, F., & Heintz, N. (2002) · Neuron · doi:10.1016/s0896-6273(02)00861-9 · Cited by 306 · see citing works
Eskelinen, E., Schmidt, C. K., Neu, S., Willenborg, M., Fuertes, G., Salvador-Montoliu, N., Tanaka, Y., Lüllmann‐Rauch, R., Hartmann, D., Heeren, J., et al. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-02-0103 · Cited by 266 · see citing works
Purkinje cell degeneration ( pcd ) Phenotypes Caused by Mutations in the Axotomy-Induced Gene, Nna1
Fernandez‐Gonzalez, A., Spada, A. R. L., Treadaway, J., Higdon, J., Harris, B. S., Sidman, R. L., Morgan, J. I., & Zuo, J. (2002) · Science · doi:10.1126/science.1068912 · Cited by 247 · see citing works
Custer, S. K., Garden, G. A., Gill, N., Rueb, U., Libby, R. T., Schultz, C., Guyenet, S. J., Deller, T., Westrum, L. E., Sopher, B. L., et al. (2006) · Nature Neuroscience · doi:10.1038/nn1750 · Cited by 240 · see citing works
Self-citationNishiyama, J., Miura, E., Mizushima, N., Watanabe, M., & Yuzaki, M. (2007) · Autophagy · doi:10.4161/auto.4964 · Cited by 159 · see citing works
Cataldo, A. M., Peterhoff, C. M., Schmidt, S. D., Terio, N. B., Duff, K., Beard, M. E., Mathews, P. M., & Nixon, R. A. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.8.821 · Cited by 157 · see citing works
Site of pcd gene action and Purkinje cell mosaicism in cerebella of chimaeric mice
Mullen, R. J. (1977) · Nature · doi:10.1038/270245a0 · Cited by 133 · see citing works
LaVail, M. M., Blanks, J. C., & Mullen, R. J. (1982) · The Journal of Comparative Neurology · doi:10.1002/cne.902120302 · Cited by 118 · see citing works
Nnal‐like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily
de la Vega, M. R., Sevilla, R. G., Hermoso, A., Lorenzo, J., Tanco, S., Díez, A., Fricker, L. D., Bautista, J. M., & Avilés, F. X. (2007) · The FASEB Journal · doi:10.1096/fj.06-7330com · Cited by 116 · see citing works
Harris, A. E., Morgan, J. I., Pecot, M., Soumare, A., Osborne, A., & Soares, H. D. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0900 · Cited by 115 · see citing works
Different Fates of Mitochondria: Alternative Ways for Degradation?
Mijaljica, D., Prescott, M., & Devenish, R. J. (2007) · Autophagy · doi:10.4161/auto.3011 · Cited by 103 · see citing works
O’Gorman, S., & Sidman, R. L. (1985) · The Journal of Comparative Neurology · doi:10.1002/cne.902340302 · Cited by 89 · see citing works
Neurodegeneration inLurcherMice Occurs via Multiple Cell Death Pathways
Doughty, M. L., Jager, P. L. D., Korsmeyer, S. J., & Heintz, N. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-10-03687.2000 · Cited by 88 · see citing works
Lurcher GRID2-Induced Death and Depolarization Can Be Dissociated in Cerebellar Purkinje Cells
Selimi, F., Lohof, A. M., Heitz, S., Lalouette, A., Jarvis, C. I., Bailly, Y. J. R., & Mariani, J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00093-x · Cited by 78 · see citing works
Selimi, F., Vogel, M. W., & Mariani, J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-14-05339.2000 · Cited by 60 · see citing works
Chakrabarti, L., Eng, J., Martinez, R. A., Jackson, S. M., Huang, J., Possin, D. E., Sopher, B. L., & Spada, A. R. L. (2008) · Vision Research · doi:10.1016/j.visres.2008.05.026 · Cited by 39 · see citing works
Self-citationChakrabarti, L., Neal, J. T., Miles, M., Martinez, R. A., Smith, A. C., Sopher, B. L., & Spada, A. R. L. (2006) · Mammalian Genome · doi:10.1007/s00335-005-0096-x · Cited by 38 · see citing works
Self-citationHandel, M. A., & Dawson, M. (1981) · Gamete Research · doi:10.1002/mrd.1120040303 · Cited by 36 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond
Bingol, B., & Sheng, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.015 · Cited by 333 · see citing works
Shehata, M., Matsumura, H., Okubo-Suzuki, R., Ohkawa, N., & Inokuchi, K. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4533-11.2012 · Cited by 285 · see citing works
BNIP3 Interacting with LC3 Triggers Excessive Mitophagy in Delayed Neuronal Death in Stroke
Shi, R., Zhu, S., Li, V., Gibson, S. B., Xu, X., & Kong, J. (2014) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12325 · Cited by 279 · see citing works
The Role of Mitophagy in Innate Immunity
Gkikas, I., Palikaras, K., & Tavernarakis, N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01283 · Cited by 244 · see citing works
Mitochondrial diseases: from molecular mechanisms to therapeutic advances
Wen, H., Deng, H., Li, B., Chen, J., Zhu, J., Zhang, X., Yoshida, S., & Zhou, Y. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02044-3 · Cited by 250 · see citing works
Lee, S.-J., & Koh, J. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-30 · Cited by 216 · see citing works
Guo, X., Sun, X., Hu, D., Wang, Y.-J., Fujioka, H., Vyas, R., Chakrapani, S., Joshi, A. U., Luo, Y., Mochly-Rosen, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms12646 · Cited by 200 · see citing works
Chu, C. T. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq143 · Cited by 167 · see citing works
Caspase-3 Mediated Cell Death in the Normal Development of the Mammalian Cerebellum
Lossi, L., Castagna, C., & Merighi, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123999 · Cited by 168 · see citing works
Autophagy regulates endoplasmic reticulum stress in ischemic preconditioning
Sheng, R., Liu, X.-Q., Zhang, L.-S., Gao, B., Han, R., Wu, Y.-Q., Zhang, X., & Qin, Z. (2012) · Autophagy · doi:10.4161/auto.18673 · Cited by 155 · see citing works
Autophagy in axonal and dendritic degeneration
Yang, Y., Coleman, M. P., Zhang, L., Zheng, X., & Yue, Z. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.04.001 · Cited by 144 · see citing works
Autophagy and the degradation of mitochondria
Goldman, S. J., Taylor, R., Zhang, Y., & Jin, S. V. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.01.005 · Cited by 145 · see citing works
Fricker, L. D. (2010) · Molecular BioSystems · doi:10.1039/c003317k · Cited by 141 · see citing works
Pi, H., Xu, S., Zhang, L., Guo, P., Li, Y., Xie, J., Tian, L., He, M., Lu, Y., Li, M., et al. (2013) · Autophagy · doi:10.4161/auto.25665 · Cited by 139 · see citing works
Sepulveda-Falla, D., Barrera-Ocampo, A., Hagel, C., Korwitz, A., Vinueza-Veloz, M. F., Zhou, K., Schonewille, M., Zhou, H., Velazquez-Perez, L., Rodriguez-Labrada, R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci66407 · Cited by 135 · see citing works
Mitochondrial autophagy in neural function, neurodegenerative disease, neuron cell death, and aging
Batlevi, Y., & Spada, A. R. L. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.09.009 · Cited by 131 · see citing works
Consensus Paper: Pathological Mechanisms Underlying Neurodegeneration in Spinocerebellar Ataxias
Matilla‐Dueñas, A., Ashizawa, T., Brice, A., Magri, S., McFarland, K. N., Pandolfo, M., Pulst, S. M., Rieß, O., Rubinsztein, D. C., Schmidt, J., et al. (2013) · The Cerebellum · doi:10.1007/s12311-013-0539-y · Cited by 128 · see citing works
Zhu, J., Gusdon, A. M., Çimen, H., Houten, B. V., Koç, E., & Chu, C. T. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.46 · Cited by 109 · see citing works
Pollard, A. K., Craig, E. L., & Chakrabarti, L. (2016) · PLOS ONE · doi:10.1371/journal.pone.0157405 · Cited by 94 · see citing works
Self-citationAD-linked, toxic NH2 human tau affects the quality control of mitochondria in neurons
Amadoro, G., Corsetti, V., Florenzano, F., Atlante, A., Ciotti, M. T., Mongiardi, M. P., Bussani, R., Nicolin, V., Nori, S. L., Campanella, M., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.10.018 · Cited by 85 · see citing works
Gao, B., Zhang, X., Han, R., Zhang, T., Chen, C., Qin, Z., & Sheng, R. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.34 · Cited by 85 · see citing works
From mice to men: lessons from mutant ataxic mice
Cendelín, J. (2014) · Cerebellum & Ataxias · doi:10.1186/2053-8871-1-4 · Cited by 83 · see citing works
Selective autophagy as a therapeutic target for neurological diseases
Xu, W., Ocak, U., Gao, L., Tu, S., Lenahan, C., Zhang, J., & Shao, A. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03667-9 · Cited by 82 · see citing works
Nanomaterial-mediated autophagy: coexisting hazard and health benefits in biomedicine
Feng, X., Zhang, Y., Zhang, C., Lai, X., Zhang, Y., Wu, J., Hu, C., & Shao, L. (2020) · Particle and Fibre Toxicology · doi:10.1186/s12989-020-00372-0 · Cited by 75 · see citing works
Mechanism and Regulation of Autophagy and Its Role in Neuronal Diseases
Hu, Z., Yang, B., Mo, X., & Xiao, H. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8921-4 · Cited by 68 · see citing works
SETX (senataxin), the helicase mutated in AOA2 and ALS4, functions in autophagy regulation
Richard, P., Feng, S., Tsai, Y.-L., Li, W., Rinchetti, P., Muhith, U., Irizarry-Cole, J., Stolz, K., Sanz, L. A., Hartono, S. R., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1796292 · Cited by 68 · see citing works
Yang, S., Xia, C., Li, S., Du, L., Zhang, L., & Hu, Y. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.184 · Cited by 65 · see citing works
Paradoxical Mitophagy Regulation by PINK1 and TUFm
Lin, J., Chen, K., Chen, W., Yao, Y., Ni, S., Ye, M., Zhuang, G., Hu, M., Gao, J., Gao, C., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.007 · Cited by 61 · see citing works
Pollard, A. K., Shephard, F., Freed, J., Liddell, S., & Chakrabarti, L. (2016) · Aging · doi:10.18632/aging.101064 · Cited by 60 · see citing works
Self-citationBaltanás, F. C., Casafont, Í., Lafarga, V., Weruaga, E., Alonso, J. R., Berciano, M. T., & Lafarga, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.246041 · Cited by 60 · see citing works
Berezniuk, I., Sironi, J., Callaway, M. B., de Castro, L. M., Hirata, I. Y., Ferro, E. S., & Fricker, L. D. (2010) · The FASEB Journal · doi:10.1096/fj.09-147942 · Cited by 60 · see citing works
A mitochondrial location for haemoglobins—Dynamic distribution in ageing and Parkinson's disease
Shephard, F., Greville‐Heygate, O., Marsh, O., Anderson, S. H., & Chakrabarti, L. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.12.001 · Cited by 58 · see citing works
Self-citationMitochondrial Mechanisms of Neuroglobin’s Neuroprotection
Yu, Z., Poppe, J. L., & Wang, X. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/756989 · Cited by 58 · see citing works
Zhang, X., Zhang, T.-T., Song, D., Zhou, J. H., Han, R., Qin, Z., & Sheng, R. (2015) · Molecular Brain · doi:10.1186/s13041-015-0112-3 · Cited by 57 · see citing works
Autophagy induction halts axonal degeneration in a mouse model of X-adrenoleukodystrophy
Launay, N., Aguado, C., Fourcade, S., Ruíz, M., Grau, L., Riera, J., Guilera, C., Girós, M., Ferrer, I., Knecht, E., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1378-8 · Cited by 52 · see citing works
Qi, Y., Ma, R., Li, X., Lv, S., Liu, X.-Y., Abulikemu, A., Zhao, X., Li, Y.-B., Guo, C.-X., & Sun, Z. (2020) · Nanoscale · doi:10.1039/d0nr01893g · Cited by 40 · see citing works
Expression of Ambra1 in mouse brain during physiological and Alzheimer type aging
Sepe, S., Nardacci, R., Fanelli, F., Rosso, P., Bernardi, C., Cecconi, F., Mastroberardino, P. G., Piacentini, M., & Moreno, S. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.07.001 · Cited by 48 · see citing works
AβPP/PS1 Transgenic Mice Show Sex Differences in the Cerebellum Associated with Aging
Ordóñez‐Gutiérrez, L., Fernandez-Perez, I., Herrera, J. L., Anton, M., Benito‐Cuesta, I., & Wandosell, F. G. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160572 · Cited by 45 · see citing works
CCP1 promotes mitochondrial fusion and motility to prevent Purkinje cell neuron loss in pcd mice
Gilmore-Hall, S. K., Kuo, J., Ward, J. M., Zahra, R., Morrison, R. S., Perkins, G. A., & Spada, A. R. L. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201709028 · Cited by 46 · see citing works
Chakrabarti, L., Zahra, R., Jackson, S. M., Kazemi‐Esfarjani, P., Sopher, B. L., Mason, A. G., Toneff, T., Ryu, S., Shaffer, S. A., Kansy, J. W., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.05.024 · Cited by 44 · see citing works
Self-citationHiggins, G. C., Devenish, R. J., Beart, P. M., & Nagley, P. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0667-9 · Cited by 44 · see citing works
Lieberman, O. J., Cartocci, V., Pigulevskiy, I., Molinari, M., Carbonell, J., Broseta, M. B., Post, M. R., Sulzer, D., Borgkvist, A., & Santini, E. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00070 · Cited by 47 · see citing works
Preconditioning Stimuli Induce Autophagy via Sphingosine Kinase 2 in Mouse Cortical Neurons
Sheng, R., Zhang, T. T., Felice, V. D., Qin, T., Qin, Z.-H., Smith, C. D., Sapp, E., DiFiglia, M., & Waeber, C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.578120 · Cited by 43 · see citing works
Ex Vivo Imaging of Excised Tissue Using Vital Dyes and Confocal Microscopy
Johnson, S. C., & Rabinovitch, P. S. (2012) · Current Protocols in Cytometry · doi:10.1002/0471142956.cy0939s61 · Cited by 42 · see citing works
Proteostasis in striatal cells and selective neurodegeneration in Huntington’s disease
Margulis, J., & Finkbeiner, S. M. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00218 · Cited by 40 · see citing works
PEX5 regulates autophagy via the mTORC1-TFEB axis during starvation
Eun, S. Y., Lee, J. N., Nam, I.-K., Liu, Z., So, H., Choe, S., & Park, R. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-017-0007-8 · Cited by 38 · see citing works
Wang, J., Han, D. K., Sun, M., & Feng, J. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0724-9 · Cited by 35 · see citing works
Estrogen deficiency induces memory loss via altered hippocampal HB-EGF and autophagy
Pandey, R., Shukla, P., Anjum, B., Gupta, H. P., Pal, S., Arjaria, N., Gupta, K., Chattopadhyay, N., Sinha, R. A., & Bandyopadhyay, S. (2019) · Journal of Endocrinology · doi:10.1530/joe-19-0197 · Cited by 35 · see citing works
Au, A. K., Chen, Y., Du, L., Smith, C. M., Manole, M. D., Baltagi, S. A., Chu, C. T., Aneja, R. K., Bayır, H., Kochanek, P. M., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.06.007 · Cited by 35 · see citing works
Tanco, S., Tort, O., Demol, H., Avilés, F. X., Gevaert, K., Damme, P. V., & Lorenzo, J. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.040360 · Cited by 33 · see citing works
The HERC2 ubiquitin ligase is essential for embryonic development and regulates motor coordination
Cubillos‐Rojas, M., Schneider, T., Hadjebi, O., Pedrazza, L., de Oliveira, J. R., Vives, F. L., Guénet, J., Duran, J., de Anta, J. M., Alcántara, S., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.11270 · Cited by 32 · see citing works
Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival
Redmann, V., Lamb, C. A., Hwang, S., Orchard, R. C., Kim, S., Razi, M., Milam, A., Park, S., Yokoyama, C. C., Kambal, A., et al. (2016) · Scientific Reports · doi:10.1038/srep23326 · Cited by 31 · see citing works
Proteomic profiling of mitochondria: what does it tell us about the ageing brain?
Ingram, T. L., & Chakrabarti, L. (2016) · Aging · doi:10.18632/aging.101131 · Cited by 31 · see citing works
Self-citationBaltanás, F. C., Berciano, M. T., Valero, J., Gómez, C., Díaz, D., Alonso, J. R., Lafarga, M., & Weruaga, E. (2012) · Glia · doi:10.1002/glia.22431 · Cited by 31 · see citing works
A structural and functional analysis of Nna1 in Purkinje cell degeneration ( pcd ) mice
Wu, H., Wang, T., Li, L., Correia, K. M., & Morgan, J. I. (2012) · The FASEB Journal · doi:10.1096/fj.12-205047 · Cited by 30 · see citing works
The potential of mitochondrial modulation by neuroglobin in treatment of neurological disorders
Gorabi, A. M., Aslani, S., Barreto, G. E., Báez-Jurado, E., Kiaie, N., Jamialahmadi, T., & Sahebkar, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.11.002 · Cited by 29 · see citing works
CHIP Is an Essential Determinant of Neuronal Mitochondrial Stress Signaling
Palubinsky, A. M., Stankowski, J. N., Kale, A. C., Codreanu, S. G., Singer, R. J., Liebler, D. C., Stanwood, G. D., & McLaughlin, B. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6102 · Cited by 29 · see citing works
Bailey, K., Balaei, M. R., Mannan, A. U., Bigio, M. R. D., & Marzban, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094327 · Cited by 29 · see citing works
Zhou, L., Hossain, M. I., Yamazaki, M., Abe, M., Natsume, R., Konno, K., Kageyama, S., Komatsu, M., Watanabe, M., Sakimura, K., et al. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14591 · Cited by 28 · see citing works
Cummins, N., Bartlett, C. A., Archer, M. A., Bartlett, E., Hemmi, J. M., Harvey, A. R., Dunlop, S. A., & Fitzgerald, M. (2013) · BMC Neuroscience · doi:10.1186/1471-2202-14-98 · Cited by 27 · see citing works
Analysis of Mitochondrial haemoglobin in Parkinson's disease brain
Shephard, F., Greville‐Heygate, O., Liddell, S., Emes, R. D., & Chakrabarti, L. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.05.001 · Cited by 27 · see citing works
Self-citationMitochondrial damage and impaired mitophagy contribute to disease progression in SCA6
Leung, T. C. S., Fields, E., Rana, N., Shen, R. Y. L., Bernstein, A. E., Cook, A. A., Phillips, D. E., & Watt, A. J. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02680-z · Cited by 25 · see citing works
A neuronal aging pattern unique to humans and common chimpanzees
Gilissen, E., Leroy, K., Yilmaz, Z., Kövari, E., Bouras, C., Boom, A., Poncelet, L., ERWIN, J. M., Sherwood, C. C., Hof, P. R., et al. (2014) · Brain Structure and Function · doi:10.1007/s00429-014-0931-5 · Cited by 25 · see citing works
Blosa, M., Bursch, C., Weigel, S., Holzer, M., Jäger, C., Janke, C., Matthews, R. T., Arendt, T., & Morawski, M. (2015) · Neural Plasticity · doi:10.1155/2016/2828536 · Cited by 25 · see citing works
Quantitative Peptidomics of Purkinje Cell Degeneration Mice
Berezniuk, I., Sironi, J., Wardman, J. H., Pasek, R. C., Berbari, N. F., Yoder, B. K., & Fricker, L. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060981 · Cited by 24 · see citing works
Takagishi, Y., Katanosaka, K., Mizoguchi, H., & Murata, Y. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.03.020 · Cited by 24 · see citing works
Distinct Types of Lipofuscin Pigment in the Hippocampus and Cerebellum of Aged Cheirogaleid Primates
Gilissen, E., & Staneva-Dobrovski, L. (2013) · The Anatomical Record · doi:10.1002/ar.22809 · Cited by 23 · see citing works
Renault, L. H., Philippe, L., Piquemal, M., & Ciapa, B. (2013) · Autophagy · doi:10.4161/auto.25712 · Cited by 23 · see citing works
Streptococcus lutetiensis Induces Autophagy via Oxidative Stress in Bovine Mammary Epithelial Cells
Chen, P., Yang, J., Wu, N., Han, B., Kastelic, J. P., & Gao, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2549772 · Cited by 21 · see citing works
Cerebellar Expression of the Neurotrophin Receptor p75 in Naked-Ataxia Mutant Mouse
Balaei, M. R., Jiao, X., Ashtari, N., Afsharinezhad, P., Ghavami, S., & Marzban, H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17010115 · Cited by 21 · see citing works
Vegh, C., Stokes, K., Ma, D., Wear, D., Cohen, J. S., Ray, S. D., & Pandey, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181230 · Cited by 19 · see citing works
Castagna, C., Merighi, A., & Lossi, L. (2016) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2016.01.010 · Cited by 18 · see citing works
Wang, J., Han, D. K., Sun, M., & Feng, J. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5747 · Cited by 18 · see citing works
Macroautophagy Abnormality in Essential Tremor
Kuo, S., Tang, G., Ma, K., Babij, R., Cortes, E. P., Vonsattel, J., Faust, P. L., Sulzer, D. L., & Louis, E. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053040 · Cited by 18 · see citing works
Yu, D., Li, M., Nie, P., Ni, B., Zhang, Z., & Zhou, Y. (2018) · Journal of Neurotrauma · doi:10.1089/neu.2017.5280 · Cited by 17 · see citing works
NIX Mediates Mitophagy in Spinal Cord Injury in Rats by Interacting with LC3
Nie, P., Wang, H., Yu, D., Wu, H., Ni, B., Kong, J., & Zhang, Z. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01082-7 · Cited by 16 · see citing works
Elarab, S. M. E., Alsafy, M., El‐Gendy, S. A. A., El‐Bakary, N. E. R., Noreldin, A. E., & Rashwan, A. M. (2024) · Journal of Experimental Zoology Part A Ecological and Integrative Physiology · doi:10.1002/jez.2782 · Cited by 13 · see citing works
Araki, A., Maruyama, R., Harada, Y., Ishikawa, N., & Harada, T. (2012) · Pathology International · doi:10.1111/j.1440-1827.2012.02861.x · Cited by 11 · see citing works
Zhu, Y., Luan, P., Liu, X., Bao, J., Liu, Q., Cai, J., Yang, J., & Zhang, Z. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.113053 · Cited by 11 · see citing works
Embryonic Cerebellar Graft Morphology Differs in Two Mouse Models of Cerebellar Degeneration
Purkartová, Z., Tichánek, F., Kolinko, Y., & Cendelín, J. (2019) · The Cerebellum · doi:10.1007/s12311-019-01067-9 · Cited by 11 · see citing works
Yang, Z., & Wang, J. (2013) · The Cerebellum · doi:10.1007/s12311-013-0499-2 · Cited by 10 · see citing works
Jan Evangelista Purkyně and the Cerebellum Then and Now
Vožeh, F. (2015) · Physiological Research · doi:10.33549/physiolres.933231 · Cited by 8 · see citing works
Nishiyama, H., Nishiyama, N., & Zemelman, B. V. (2024) · The Journal of Physiology · doi:10.1113/jp285887 · Cited by 9 · see citing works
Bibliometric insights into the inflammation and mitochondrial stress in ischemic stroke
Wang, C., Gu, L., Zhang, Y., Gao, Y., Jian, Z., & Xiong, X. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114845 · Cited by 7 · see citing works
Mitochondrial Regulation of Cell Death
Liu, D., Perfettini, J., & Brenner, C. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_6 · Cited by 7 · see citing works
The Critical Role of Autophagy and Phagocytosis in the Aging Brain
Bondy, S. C., & Wu, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010057 · Cited by 5 · see citing works
Sox-positive cell population in the adult cerebellum increases upon tissue degeneration
Salih, S., Nizamudeen, Z. A., Melo, N. D., Chakrabarti, L., & Sottile, V. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113950 · Cited by 5 · see citing works
Self-citationvan Noort, S. A. M., van der Veen, S., de Koning, T. J., Tijssen, M. A. J., Verbeek, D. S., & Sival, D. A. (2023) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2023.05.009 · Cited by 5 · see citing works
Autophagy in different flavors: Dysregulated protein degradation in neurological diseases
Chu, C. T. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.03.020 · Cited by 5 · see citing works
mTOR suppresses macroautophagy during postnatal development of the striatumPreprint
Lieberman, O. J., Pigulevskiy, I., Post, M. R., Sulzer, D. L., & Santini, E. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/536680 · Cited by 5 · see citing works
Single-nucleus multiome analysis of human cerebellum in Alzheimer’s disease-related dementiaPreprint
Cheng, F., Feng, Y., Flanagan, M. E., Bonakdarpour, B., Jamshidi, P., Castellani, R. J., Mao, Q., Chu, X., Gao, H., Liu, Y., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4871032/v1 · Cited by 5 · see citing works
Fields, E., Rogers, B. C., Leung, T. C. S., Huang, A., Kern, M., Kontowicz, N., Dolin, H., & Watt, A. J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2525795122 · Cited by 3 · see citing works
Apoptosis, Autophagy, and Unfolded Protein Response and Cerebellar Development
Moosavi, M. A., Rahmati, M., Ashtari, N., Alizadeh, J., Hashemi, M. M., Bathaei, S. Z., & Ghavami, S. (2017) · Contemporary clinical neuroscience · doi:10.1007/978-3-319-59749-2_8 · Cited by 3 · see citing works
Reduction of Microvessel Number and Length in the Cerebellum of Purkinje Cell Degeneration Mice
Kolinko, Y., Králíčková, M., & Cendelín, J. (2023) · The Cerebellum · doi:10.1007/s12311-023-01556-y · Cited by 3 · see citing works
Earnshaw, R., Zhang, Y. T., Heymann, G., Fujisawa, K., Hui, S., Kapadia, M., Kalia, L. V., & Kalia, S. K. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106625 · Cited by 2 · see citing works
Xie, L., Cai, Y., Chen, B., Li, B., Zou, J., & Xu, H. (2025) · Advanced Science · doi:10.1002/advs.202500438 · Cited by 2 · see citing works
Cerebellar Biochemistry/Pharmacology
Seki, T. (2023) · Contemporary clinical neuroscience · doi:10.1007/978-3-031-24345-5_3 · Cited by 1 · see citing works
MAINTAINING AUTOPHAGIC BALANCE: A ROLE FOR BRAKES
Cherra, S. J., & Chu, C. T. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0005 · Cited by 1 · see citing works
Apoptosis, Autophagy, and Unfolded Protein Response and Cerebellar Development
Behrooz, A. B., Rahmati, M., Talaie, Z., Ashtari, N., Alizadeh, J., Hashemi, M. M., Bathaie, S. Z., Moosavi, M. A., & Ghavami, S. (2023) · Contemporary clinical neuroscience · doi:10.1007/978-3-031-23104-9_11 · Cited by 1 · see citing works
Akita, K. (2016) · Springer eBooks · doi:10.1007/978-3-319-24551-5_61
- Authors
- Chakrabarti, L., Eng, J., Ivanov, N., Garden, G. A., & La Spada, A. R.
- Affiliations
- University of Washington (US)
- Venue
- Molecular Brain
- Published
- 2009-07-29
- Volume
- 2
- Issue
- 1
- Pages
- 24-24
- ISSN
- 1756-6606 (ISSN-L)
- PMC
- PMC2729476
- OpenAlex
- W2028695079
- Cited by
- 112
- References
- 36
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 7 · 2023: 5 · 2022: 1 · 2021: 4 · 2020: 8 · 2019: 5 · 2018: 7 · 2017: 1 · 2016: 15 · 2015: 5 · 2014: 13 · 2013: 13 · 2012: 10
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular Brain (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (EY-01730, HD02274)
- Intellectual and Developmental Disabilities Research Center
- National Eye Institute (EY 18106, EY-01730, R01EY014997, R21EY018106, P30EY001730, EY 14997)
- National Institute of Neurological Disorders and Stroke (R01NS052535)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD02274, P30HD002274)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- Purkinje cells, Purkinje cell degeneration, autophagy, mitophagy, neuronal cell death, Bax, apoptosis, LC3, p62, cerebellum, hereditary ataxia, neurodegeneration
- MeSH terms
- Animals, Ataxia, Autophagy, Dendrites, Endoplasmic Reticulum, Mice, Neurologic Mutants, Mitochondria, Nerve Degeneration, Phagosomes, Phenotype, Purkinje Cells, bcl-2-Associated X Protein, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review