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Neuronal mitochondria transport Pink1 mRNA via synaptojanin 2 to support local mitophagy
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Abstract
PTEN-induced kinase 1 (PINK1) is a short-lived protein required for the removal of damaged mitochondria through Parkin translocation and mitophagy. Because the short half-life of PINK1 limits its ability to be trafficked into neurites, local translation is required for this mitophagy pathway to be active far from the soma. The Pink1 transcript is associated and cotransported with neuronal mitochondria. In concert with translation, the mitochondrial outer membrane proteins synaptojanin 2 binding protein (SYNJ2BP) and synaptojanin 2 (SYNJ2) are required for tethering Pink1 mRNA to mitochondria via an RNA-binding domain in SYNJ2. This neuron-specific adaptation for the local translation of PINK1 provides distal mitochondria with a continuous supply of PINK1 for the activation of mitophagy.
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1 retracted
RETRACTED ARTICLE: Parkin and PINK1 mitigate STING-induced inflammation
Sliter, D. A., Martinez, J., Hao, L., Chen, X., Sun, N., Fischer, T. D., Burman, J. L., Li, Y., Zhang, Z., Narendra, D. P., et al. (2018) · Nature · doi:10.1038/s41586-018-0448-9 · Cited by 1,287
RetractedSTAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn923 · Cited by 14,108
Enzymatic assembly of DNA molecules up to several hundred kilobases
Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009) · Nature Methods · doi:10.1038/nmeth.1318 · Cited by 10,088
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944
The ImageJ ecosystem: An open platform for biomedical image analysis
Schindelin, J., Rueden, C., Hiner, M., & Eliceiri, K. W. (2015) · Molecular Reproduction and Development · doi:10.1002/mrd.22489 · Cited by 2,717
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
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Narendra, D. P., & Youle, R. J. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01513-9 · Cited by 600
Mitochondria at the crossroads of health and disease
Suomalainen, A., & Nunnari, J. M. (2024) · Cell · doi:10.1016/j.cell.2024.04.037 · Cited by 528
Mitochondrial heterogeneity and homeostasis through the lens of a neuron
Pekkurnaz, G., & Wang, X. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00594-w · Cited by 201
Targeting mitophagy in neurodegenerative diseases
Antico, O., Thompson, P. W., Hertz, N. T., Muqit, M. M. K., & Parton, L. E. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01105-0 · Cited by 187
Disruption of axonal transport in neurodegeneration
Berth, S. H., & Lloyd, T. E. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168554 · Cited by 135
De-centralizing the Central Dogma: mRNA translation in space and time
Bourke, A. M., Schwarz, A., & Schuman, E. M. (2023) · Molecular Cell · doi:10.1016/j.molcel.2022.12.030 · Cited by 106
Mitophagy in the pathogenesis and management of disease
Wang, Q., Sun, Y., Li, T. Y., & Auwerx, J. (2026) · Cell Research · doi:10.1038/s41422-025-01203-7 · Cited by 103
Mitophagy in the retina: Viewing mitochondrial homeostasis through a new lens
Jiménez‐Loygorri, J. I., Benítez‐Fernández, R., Viedma-Poyatos, Á., Zapata‐Muñoz, J., Villarejo‐Zori, B., Gómez‐Sintes, R., & Boya, P. (2023) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2023.101205 · Cited by 84
De Pace, R., Ghosh, S., Ryan, V. H., Sohn, M., Jarnik, M., Rezvan Sangsari, P., Morgan, N. Y., Dale, R. K., Ward, M. E., & Bonifacino, J. S. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01619-1 · Cited by 81
Eldeeb, M. A., Bayne, A. N., Fallahi, A., Goiran, T., MacDougall, E. J., Soumbasis, A., Zorca, C. E., Jones-Tabah, J., Thomas, R. A., Karpilovsky, N. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313540121 · Cited by 81
Piol, D., Robberechts, T., & Cruz, S. D. (2023) · Neuron · doi:10.1016/j.neuron.2023.02.028 · Cited by 68
RNA granules in neuronal plasticity and disease
Bauer, K. E., de Queiroz, B. R., Kiebler, M. A., & Besse, F. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.04.004 · Cited by 60
Structural Mechanisms of Mitochondrial Quality Control Mediated by PINK1 and Parkin
Trempe, J., & Gehring, K. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168090 · Cited by 63
Mechanistic insights into the basis of widespread RNA localization
Chekulaeva, M. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01444-5 · Cited by 51
Linking transport and translation of mRNAs with endosomes and mitochondria
Müntjes, K., Devan, S.-K., Reichert, A. S., & Feldbrügge, M. (2021) · EMBO Reports · doi:10.15252/embr.202152445 · Cited by 50
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Hees, J. T., & Harbauer, A. B. (2022) · Biomolecules · doi:10.3390/biom12111595 · Cited by 53
Self-citationDiverse routes to mitophagy governed by ubiquitylation and mitochondrial import
Clague, M. J., & Urbé, S. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.01.003 · Cited by 55
FMRP regulates MFF translation to locally direct mitochondrial fission in neurons
Fenton, A. R., Peng, R., Bond, C., Hugelier, S., Lakadamyali, M., Chang, Y., Holzbaur, E. L. F., & Jongens, T. A. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01544-2 · Cited by 49
Calcium-mediated regulation of mitophagy: implications in neurodegenerative diseases
Borbolis, F., Ploumi, C., & Palikaras, K. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00049-2 · Cited by 50
Hees, J. T., Wanderoy, S., Lindner, J., Helms, M., Mahadevan, H. M., & Harbauer, A. B. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01007-w · Cited by 53
Self-citationKoppers, M., Özkan, N., Nguyen, H. H., Jurriens, D., McCaughey, J., Nguyen, D. T. M., Li, C. H., Stucchi, R., Altelaar, M., MacGillavry, H. D., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.05.005 · Cited by 44
Cohen, B., Altman, T., Golani‐Armon, A., Savulescu, A. F., Ibraheem, A., Mhlanga, M. M., Perlson, E., & Arava, Y. (2022) · Journal of Cell Science · doi:10.1242/jcs.259436 · Cited by 38
Hallmarks and Molecular Tools for the Study of Mitophagy in Parkinson’s Disease
Goiran, T., Eldeeb, M. A., Zorca, C. E., & Fon, E. A. (2022) · Cells · doi:10.3390/cells11132097 · Cited by 38
Cassella, L., & Ephrussi, A. (2022) · Nature Communications · doi:10.1038/s41467-022-34004-2 · Cited by 36
Hitchhiking Across Kingdoms: Cotransport of Cargos in Fungal, Animal, and Plant Cells
Christensen, J. R., & Reck‐Peterson, S. L. (2022) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120420-104341 · Cited by 33
A unified mechanism for mitochondrial damage sensing in PINK1-Parkin–mediated mitophagy
Thayer, J. A., Petersen, J. D., Huang, X., Budet, L. M. G., Hawrot, J., Ramos, D. M., Sekine, S., Li, Y., Ward, M. E., & Narendra, D. P. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00604-z · Cited by 37
Role of Mitochondria–ER Contact Sites in Mitophagy
Rühmkorf, A., & Harbauer, A. B. (2023) · Biomolecules · doi:10.3390/biom13081198 · Cited by 35
Self-citationWang, M., Wei, R., Li, G., Bi, H.-L., Jia, Z., Zhang, M., Pang, M., Li, X., Ma, L., & Tang, Y. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215871 · Cited by 31
Mitophagy in intracerebral hemorrhage: a new target for therapeutic intervention
Chen, Y., Tang, W., Huang, X., An, Y., Li, J., Yuan, S., Shan, H., & Zhang, M. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.379019 · Cited by 26
PINK1 is a target of T cell responses in Parkinson’s disease
Williams, G. P., Freuchet, A., Michaelis, T., Frazier, A., Tran, N. K., Lima-Júnior, J. R., Phillips, E. J., Mallal, S. A., Litvan, I., Goldman, J. G., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci180478 · Cited by 34
Coupling axonal mRNA transport and local translation to organelle maintenance and function
Vargas, J. N. S., Sleigh, J. N., & Schiavo, G. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.01.008 · Cited by 24
Ionescu, A., Altman, T., & Perlson, E. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00623-6 · Cited by 23
Zaninello, M., Schlegel, T., Nolte, H., Pirzada, M., Savino, E., Barth, E., Klein, I., Wüstenberg, H., Uddin, T., Wolff, L., et al. (2024) · Science Advances · doi:10.1126/sciadv.adn2050 · Cited by 25
Bayne, A. N., Dong, J., Amiri, S., Farhan, S. M. K., & Trempe, J. (2023) · PLoS ONE · doi:10.1371/journal.pone.0284541 · Cited by 25
Ilacqua, N., Anastasia, I., Aloshyn, D., Ghandehari‐Alavijeh, R., Peluso, E. A., Brearley-Sholto, M. C., Pellegrini, L. V., Raimondi, A., Vallim, T. Q. D. A., & Pellegrini, L. (2022) · Biology Direct · doi:10.1186/s13062-022-00344-8 · Cited by 24
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Markaki, M., Tsagkari, D., & Tavernarakis, N. (2023) · Journal of Cell Science · doi:10.1242/jcs.260638 · Cited by 22
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Tingey, M., Schnell, S. J., Yu, W., Saredy, J., Junod, S. L., Patel, D., Alkurdi, A., & Yang, W. (2022) · Cells · doi:10.3390/cells11193079 · Cited by 18
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Maddison, D. C., Malik, B. R., Amadio, L., Bis‐Brewer, D. M., Zuchner, S. L., Peters, O. M., & Smith, G. A. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112883 · Cited by 20
Singh, P. K., Agarwal, S., Volpi, I., Wilhelm, L. P., Becchi, G., Keenlyside, A., Macartney, T., Toth, R. L., Rousseau, A., Masson, G. R., et al. (2025) · Science Advances · doi:10.1126/sciadv.adn2528 · Cited by 21
Huang, N., & Sheng, Z. (2022) · Cell Regeneration · doi:10.1186/s13619-022-00138-3 · Cited by 20
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Axonal mitophagy in retinal ganglion cells
Yang, L., Li, Y., Jiao, Q., Wei, M., Wang, Y., Cui, A., Li, Z., & Li, G. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01761-0 · Cited by 22
Emerging implications for ribosomes in proximity to mitochondria
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Nambiar, A., & Manjithaya, R. R. (2024) · Journal of Cell Science · doi:10.1242/jcs.260481 · Cited by 17
Currim, F., Shukla, S., Singh, J., Gohel, D., Mane, M., Shinde, A., Roy, M., Goyani, S., Vasiyani, H., Chandran, A., et al. (2024) · NeuroToxicology · doi:10.1016/j.neuro.2024.02.005 · Cited by 17
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Wang, L., Zhang, Z., Zhang, H., Zhou, M., Huang, C. Z., Xia, W., Li, J., & You, H. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1346446 · Cited by 18
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Li, T., Jin, M., Huang, L., Zhang, Y., Zong, J., Shan, H., Kang, H., Xu, M., Liu, H., Zhao, Y., et al. (2023) · Aquatic Toxicology · doi:10.1016/j.aquatox.2023.106616 · Cited by 17
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Wang, K., Chen, X., Liu, M., Li, Y., Zhu, Y., Zhou, T., Tao, W., Ma, Y., Guo, Y., Wang, L., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06611-2 · Cited by 13
Dye disaggregation light-up aptamer for super-resolution RNA imaging
Yan, C., Miao, L., Zhang, Y., Zhou, X., Wang, G., Li, Y., Qiao, Q., & Xu, Z. (2023) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2023.133731 · Cited by 12
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Song, Y., Geng, W., Zhu, D., Liang, H., Du, Z., Tong, B., Wang, K., Li, S., Gao, Y., Feng, X., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.12.028 · Cited by 12
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Zaninello, M., Baptista, P., & Duarte, F. V. (2024) · Biology · doi:10.3390/biology13090746 · Cited by 12
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Reshetniak, S., Bogaciu, C. A., Bonn, S., Brose, N., Cooper, B. H., D’Este, E., Fauth, M. J., Fernández‐Busnadiego, R., Fiošins, M., Fischer, A., et al. (2024) · The Journal of Physiology · doi:10.1113/jp286400 · Cited by 15
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Yao, M., Wang, X., Lin, H., Shu, H., Xu, Z., Tang, L., Guo, W., & Xu, P. (2024) · Inflammation · doi:10.1007/s10753-024-02219-8 · Cited by 14
Jeong, Y., Davis, C.-H. O., Muscarella, A. M., Navarro, H. H., Deshpande, V. A., Moore, L. G., Keun-young Kim, A., Ellisman, M. H., & Marsh‐Armstrong, N. (2025) · eLife · doi:10.7554/elife.103844 · Cited by 12
Luo, L., Que, M., Zeng, L., Wang, X., Sun, T., Zhou, Z., Zhao, Y., Li, S., & Luo, A. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107947 · Cited by 11
de Mello, N. P., Fecher, C., Pastor, A. M., Perocchi, F., & Misgeld, T. (2023) · Nature Protocols · doi:10.1038/s41596-023-00831-w · Cited by 11
Self-citationMulti-omics profiling identifies a deregulated FUS-MAP1B axis in ALS/FTD–associated UBQLN2 mutants
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Self-citationEndoplasmic reticulum – condensate interactions in protein synthesis and secretion
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Lu, W.-H., Chang, T.-T., Chang, Y., Liu, Y.-H., Lin, C.-H., Suen, C., Hwang, M., & Huang, Y. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01061-2 · Cited by 11
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Morisaki, T., Wiggan, O., & Stasevich, T. J. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-030822-034116 · Cited by 10
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Luo, J.-C., Feng, L., Wang, L., Fang, Z., Lang, J., & Lang, B. (2024) · Brain Circulation · doi:10.4103/bc.bc_95_23 · Cited by 9
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Bauer, V. A., & Koppers, M. (2025) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2025.102332 · Cited by 9
Autophagy at the synapse, an early site of dysfunction in neurodegeneration
Jasutkar, H. G., & Yamamoto, A. (2023) · Current Opinion in Physiology · doi:10.1016/j.cophys.2023.100631 · Cited by 9
Wang, M., Wu, Z., Zheng, X., Huang, Y., Jin, Y., Song, J., Lei, W., Liu, H., Yu, R., Yang, H., et al. (2025) · Stem Cell Research & Therapy · doi:10.1186/s13287-025-04161-4 · Cited by 9
Mitochondrial hitch-hiking of Pink1 mRNA supports axonal mitophagy
Harbauer, A. B., & Schwarz, T. L. (2022) · Autophagy · doi:10.1080/15548627.2022.2070332 · Cited by 9
Self-citationNeuronal compartmentalization results in “impoverished” axonal mitochondriaPreprint
Pastor, A. M., Lewis, L. S. C., Müller, S., Guedes-Dias, P., Olifiers, L., Pelkonen, P., Martin, A. D. R., Fecher, C., Skiba, N. P., Hao, Y., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.27.684882 · Cited by 9
Self-citationMitochondrial specialization and signaling shape neuronal function
Tong, B. C., Gubinelli, F., Burbulla, L. F., & Harbauer, A. B. (2026) · Trends in Neurosciences · doi:10.1016/j.tins.2025.12.006 · Cited by 9
Self-citationSongster, L. D., Bhuyan, D., Christensen, J. R., & Reck‐Peterson, S. L. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-01-0025 · Cited by 8
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Cavarischia-Rega, C., Sharma, K., Fitzgerald, J. C., & Maček, B. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100838 · Cited by 7
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Lam, W. K., Lindblom, R. S. J., Milky, B., Mazzachi, P., Hadian-Jazi, M., Küng, C. J., Khuu, G., Uoselis, L., Nguyen, T. N., Skulsuppaisarn, M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.09.611943 · Cited by 10
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Gu, Q., Yuan, S., An, Y., Sun, W., Xu, M., Xue, M., Li, X., Liu, C., Shan, H., & Zhang, M. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01029 · Cited by 7
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Wang, C., Zhao, M., Yue, Y., Hu, C., Zhou, C., Zhang, Z., He, Y., Luo, Y., Shen, T., Dang, S., et al. (2024) · Drug Design Development and Therapy · doi:10.2147/dddt.s478072 · Cited by 7
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Self-citationAkram, S., Zittlau, K. I., Sharma, K., Fitzgerald, J. C., Rafiq, N. M., Maček, B., & Ralf-Peter, J. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00905 · Cited by 8
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Metadata
- Authors
- Harbauer, A. B., Hees, J. T., Wanderoy, S., Segura, I., Gibbs, W., Cheng, Y., Ordonez, M., Cai, Z., Cartoni, R., Ashrafi, G., Wang, C., Perocchi, F., He, Z., & Schwarz, T. L.
- Affiliations
- Boston Children's Hospital (US)
- Max Planck Institute of Neurobiology (DE)
- Helmholtz Munich (DE)
- Corresponding author
- Harbauer, Angelika B.
- Schwarz, Thomas L.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2022-05
- Volume
- 110
- Issue
- 9
- Pages
- 1516-1531.e9
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC9081165
- OpenAlex
- W4225594780
- Cited by
- 156
- References
- 100
- Citations by year
- 2026: 26 · 2025: 40 · 2024: 44 · 2023: 25 · 2022: 17
- FWCI
- 23.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 368 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Open access LMU (Ludwid Maxmilian's Universitat Munchen) (submittedVersion)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- Site cant be reached (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Funders
- DFG (HA 7728/2-1)
- Yale University (FLAG-SYNJ2a, SYNJ1-FLAG)
- NIH (R01NS107490, P30HD018655, R01GM069808)
- Max Planck Society
- Jane Coffin Childs Memorial Fund for Medical Research
- Howard Hughes Medical Institute
- Harvard NeuroDiscovery Center (NS072030)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- PINK1, mitophagy, local translation, neuronal mitochondria, mitochondrial transport, RNA-binding domain, Parkin, neurites
- MeSH terms
- Mitochondria, Nerve Tissue Proteins, Neurons, Phosphoric Monoester Hydrolases, Protein Kinases, RNA, Messenger, Ubiquitin-Protein Ligases, Mitophagy
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