Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Open accessAbstract
PINK1 is a mitochondrial kinase mutated in some familial cases of Parkinson’s disease. It has been found to work in the same pathway as the E3 ligase Parkin in the maintenance of flight muscles and dopaminergic neurons in Drosophila melanogaster and to recruit cytosolic Parkin to mitochondria to mediate mitophagy in mammalian cells. Although PINK1 has a predicted mitochondrial import sequence, its cellular and submitochondrial localization remains unclear in part because it is rapidly degraded. In this study, we report that the mitochondrial inner membrane rhomboid protease presenilin-associated rhomboid-like protein (PARL) mediates cleavage of PINK1 dependent on mitochondrial membrane potential. In the absence of PARL, the constitutive degradation of PINK1 is inhibited, stabilizing a 60-kD form inside mitochondria. When mitochondrial membrane potential is dissipated, PINK1 accumulates as a 63-kD full-length form on the outer mitochondrial membrane, where it can recruit Parkin to impaired mitochondria. Thus, differential localization to the inner and outer mitochondrial membranes appears to regulate PINK1 stability and function.
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PINK1 stabilization on depolarized mitochondria results from impaired mitochondrial import and proteolytic processing, allowing full-length PINK1 to accumulate at the outer mitochondrial membrane.
“PINK1 stabilization on depolarized mitochondria results from impaired mitochondrial import and proteolytic processing, allowing full-length PINK1 to accumulate at the outer mitochondrial membrane [57, 58].”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [57]
PARL modulates mitophagy by degrading the mitophagy protein PINK1.
“PARL modulates mitophagy by degrading the mitophagy protein PINK1 [38].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [38]
PINK1 is constitutively degraded by mitochondrial proteases and the ubiquitin-proteasome pathway in a mitochondrial membrane potential (ΔΨm)-dependent manner.
“The PINK1 mitochondrial serine/threonine protein kinase is constitutively degraded by a combination of mitochondrial proteases and the ubiquitin-proteasome pathway in a mitochondrial membrane potential (ΔΨm)-dependent manner (Jin et al., 2010).”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Jin et al., 2010
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works
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 · see citing works
Self-citationHereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works
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 · see citing works
Self-citationPINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · see citing works
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969 · see citing works
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788 · see citing works
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705 · see citing works
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works
Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> mutants
Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works
Mitochondrial Dysfunction and Oxidative Damage in parkin-deficient Mice
Palacino, J. J., Sagi, D., Goldberg, M. S., Krauss, S., Motz, C., Wacker, M., Klose, J., & Shen, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401135200 · Cited by 995 · see citing works
Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.-W., Yang, L., Beal, M. F., Vogel, H., & Lu, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602493103 · Cited by 798 · see citing works
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 735 · see citing works
Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
Gautier, C. A., Kitada, T., & Shen, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802076105 · Cited by 698 · see citing works
PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1
Pridgeon, J. W., Olzmann, J. A., Chin, L.-S., & Li, L. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050172 · Cited by 596 · see citing works
Drosophila Rhomboid-1 Defines a Family of Putative Intramembrane Serine Proteases
Urban, S., Lee, J. R., & Freeman, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00525-6 · Cited by 564 · see citing works
Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515 · see citing works
The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
Plun‐Favreau, H., Klupsch, K., Moisoi, N., Gandhi, S., Kjaer, S., Frith, D., Harvey, K., Deas, E., Harvey, R. J., McDonald, N. Q., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1644 · Cited by 476 · see citing works
Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
Silvestri, L., Caputo, V., Bellacchio, E., Atorino, L., Dallapiccola, B., Valente, E. M., & Casari, G. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi377 · Cited by 449 · see citing works
The kinase domain of mitochondrial PINK1 faces the cytoplasm
Zhou, C. H., Huang, Y., Shao, Y., May, J., Prou, D., Perier, C., Dauer, W. T., Schon, E. A., & Przedborski, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802814105 · Cited by 312 · see citing works
Shimura, H., Hattori, N., Kubo, S., Yoshikawa, M., Kitada, T., Matsumine, H., Asakawa, S., Minoshima, S., Yamamura, Y., Shimizu, N., et al. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199905)45:5 · Cited by 282 · see citing works
Characterization of PINK1 processing, stability, and subcellular localization
Lin, W., & Kang, U. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05398.x · Cited by 261 · see citing works
Analysis of the Assembly Profiles for Mitochondrial- and Nuclear-DNA-Encoded Subunits into Complex I
Lazarou, M., McKenzie, M., Ohtake, A., Thorburn, D. R., & Ryan, M. T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00074-07 · Cited by 254 · see citing works
Self-citationUrban, S., & Freeman, M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00181-3 · Cited by 241 · see citing works
Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease
Tang, B., Xiong, H., Sun, P., Zhang, Y., Wang, D., Hu, Z., Zhu, Z.-H., Ma, H., Pan, Q., Xia, J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl104 · Cited by 213 · see citing works
Whitworth, A. J., Lee, J. R., Ho, V. M.-W., Flick, R., Chowdhury, R. B., & McQuibban, G. A. (2008) · Disease Models & Mechanisms · doi:10.1242/dmm.000109 · Cited by 188 · see citing works
Střı́šovský, K., Sharpe, H. J., & Freeman, M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.006 · Cited by 184 · see citing works
Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress
Muqit, M. M. K., Abou‐Sleiman, P. M., Saurin, A. T., Harvey, K., Gandhi, S., Deas, E., Eaton, S. D., Smith, M. D. P., Venner, K., Matilla‐Dueñas, A., et al. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03845.x · Cited by 172 · see citing works
Weihofen, A., Ostaszewski, B. L., Minami, Y., & Selkoe, D. J. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm334 · Cited by 167 · see citing works
Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1
Takatori, S., Ito, G., & Iwatsubo, T. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.10.019 · Cited by 119 · see citing works
Attila Gabor, S. I. K., Passer, B. J., Koonin, E. V., & Pellegrini, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313756200 · Cited by 66 · see citing works
Haucke, V., Santos‐Ocaña, C., Hönlinger, A., et al. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.4024 · Cited by 50 · see citing works
The PARL family of mitochondrial rhomboid proteases
Hill, R. B., & Pellegrini, L. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.12.011 · Cited by 40 · see citing works
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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works
Self-citationMitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Self-citationAn Overview of Autophagy: Morphology, Mechanism, and Regulation
Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521 · see citing works
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 · see citing works
Self-citationMitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081 · see citing works
Self-citationSarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · see citing works
Self-citationMitochondrial dynamics in health and disease: mechanisms and potential targets
Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306 · see citing works
The increasing complexity of the ubiquitin code
Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054 · see citing works
Mitophagy: mechanisms, pathophysiological roles, and analysis
Ding, W.-X., & Yin, X.-M. (2012) · bchm · doi:10.1515/hsz-2012-0119 · Cited by 1,032 · see citing works
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851 · see citing works
A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
Sugiura, A., McLelland, G., Fon, E. A., & McBride, H. M. (2014) · The EMBO Journal · doi:10.15252/embj.201488104 · Cited by 862 · see citing works
Mitochondrial Defects and Oxidative Stress in Alzheimer Disease and Parkinson Disease
Yan, M. H., Wang, X., & Zhu, X. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.014 · Cited by 718 · see citing works
Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711 · see citing works
Yun, J., & Finkel, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.011 · Cited by 626 · see citing works
PINK1/Parkin-mediated mitophagy in mammalian cells
Eiyama, A., & Okamoto, K. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.01.002 · Cited by 603 · see citing works
Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577 · see citing works
Laker, R. C., Drake, J. C., Wilson, R. J., Lira, V. A., Lewellen, B. M., Ryall, K. A., Fisher, C. C., Zhang, M., Saucerman, J. J., Goodyear, L. J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00520-9 · Cited by 529 · see citing works
Mitochondrial fission facilitates the selective mitophagy of protein aggregates
Burman, J. L., Pickles, S., Wang, C., Sekine, S., Vargas, J. N. S., Zhang, Z., Youle, A. M., Nezich, C. L., Wu, X., Hammer, J. A., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612106 · Cited by 479 · see citing works
Self-citationMitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
Receptor-mediated mitophagy in yeast and mammalian systems
Liu, L., Sakakibara, K., Chen, Q., & Okamoto, K. (2014) · Cell Research · doi:10.1038/cr.2014.75 · Cited by 421 · see citing works
Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works
Self-citationThe three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications
Durcan, T. M., & Fon, E. A. (2015) · Genes & Development · doi:10.1101/gad.262758.115 · Cited by 400 · see citing works
Mitophagy: An Emerging Role in Aging and Age-Associated Diseases
Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359 · see citing works
High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy
Hasson, S. A., Kane, L. A., Yamano, K., Huang, C.-H., Sliter, D. A., Buehler, E., Wang, C., Heman-Ackah, S. M., Hessa, T., Guha, R., et al. (2013) · Nature · doi:10.1038/nature12748 · Cited by 365 · see citing works
Self-citationRepairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Mechanisms of drug-induced liver injury
Yuan, L., & Kaplowitz, N. (2013) · Clinics in Liver Disease · doi:10.1016/j.cld.2013.07.002 · Cited by 322 · see citing works
How mitochondrial dynamism orchestrates mitophagy
Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311 · see citing works
Molecular mechanisms for mitochondrial adaptation to exercise training in skeletal muscle
Drake, J. C., Wilson, R. J., & Yan, Z. (2016) · The FASEB Journal · doi:10.1096/fj.15-276337 · Cited by 263 · see citing works
Mitochondrial degradation: Mitophagy and beyond
Uoselis, L., Nguyen, T. N., & Lazarou, M. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.08.021 · Cited by 270 · see citing works
Self-citationMitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
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Disease-associated tau impairs mitophagy by inhibiting Parkin translocation to mitochondria
Cummins, N., Tweedie, A., Zuryn, S., Bertran‐Gonzalez, J., & Götz, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899360 · Cited by 267 · see citing works
Ivankovic, D., Chau, K., Schapira, A. H. V., & Gegg, M. E. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13412 · Cited by 264 · see citing works
Mitochondrial Dysfunction in Alzheimer’s Disease and the Rationale for Bioenergetics Based Therapies
Onyango, I. G., Dennis, J., & Khan, S. M. (2016) · Aging and Disease · doi:10.14336/ad.2015.1007 · Cited by 260 · see citing works
Seirafi, M., Kozlov, G., & Gehring, K. (2015) · The FEBS Journal · doi:10.1111/febs.13249 · Cited by 256 · see citing works
Mitochondrial quality control: An integrated network of pathways
Fischer, F., Hamann, A., & Osiewacz, H. D. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.02.004 · Cited by 248 · see citing works
The ADP/ATP translocase drives mitophagy independent of nucleotide exchange
Hoshino, A., Wang, W.-J., Wada, S., McDermott-Roe, C., Evans, C. S., Gosis, B., Morley, M. P., Rathi, K. S., Li, J., Li, K., et al. (2019) · Nature · doi:10.1038/s41586-019-1667-4 · Cited by 228 · see citing works
Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation
Iguchi, M., Kujuro, Y., Okatsu, K., Koyano, F., Kosako, H., Kimura, M., Suzuki, N., Uchiyama, S., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.467530 · Cited by 209 · see citing works
Organelle-Specific Initiation of Autophagy
Sica, V., Galluzzi, L., Bravo-San Pedro, J. M., Izzo, V., Maiuri, M. C., & Kroemer, G. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.021 · Cited by 205 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Mitohormesis in exercise training
Merry, T. L., & Ristow, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.032 · Cited by 176 · see citing works
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159 · see citing works
Urolithin A improves Alzheimer's disease cognition and restores mitophagy and lysosomal functions
Hou, Y., Chu, X., Park, J., Zhu, Q., Hussain, M., Li, Z., Madsen, H. B., Yang, B., Wei, Y., Wang, Y., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13847 · Cited by 145 · see citing works
Bartolomé, A., García-Aguilar, A., Asahara, S.-I., Kido, Y., Guillén, C., Pajvani, U. B., & Benito, M. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00441-17 · Cited by 141 · see citing works
Autophagy in neurodegeneration: New insights underpinning therapy for neurological diseases
Corti, O., Blomgren, K., Poletti, A., & Beart, P. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15002 · Cited by 141 · see citing works
Role of p62/SQSTM1 in liver physiology and pathogenesis
Manley, S., Williams, J. A., & Ding, W.-X. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213489446 · Cited by 135 · see citing works
Hook, P. W., McClymont, S. A., Cannon, G. H., Law, W. D., Morton, A. J., Goff, L. A., & McCallion, A. S. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2018.02.001 · Cited by 136 · see citing works
Mitochondrial quality control by the Pink1/Parkin system
Rüb, C., Wilkening, A., & Voos, W. (2017) · Cell and Tissue Research · doi:10.1007/s00441-016-2485-8 · Cited by 132 · see citing works
Role of Parkin and endurance training on mitochondrial turnover in skeletal muscle
Chen, C. C. W., Erlich, A. T., & Hood, D. A. (2018) · Skeletal Muscle · doi:10.1186/s13395-018-0157-y · Cited by 124 · see citing works
Ahuja, P., Ng, C. F., Pang, B. P. S., Chan, W. S., Tse, M. C. L., Bi, X., Kwan, H.-L. R., Brobst, D., Herlea-Pana, O., Yang, X., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.1985257 · Cited by 116 · see citing works
Protective role of Parkin in skeletal muscle contractile and mitochondrial function
Gouspillou, G., Godin, R., Piquereau, J., Picard, M., Mofarrahi, M., Mathew, J., Purves‐Smith, F. M., Sgarioto, N., Hepple, R. T., Burelle, Y., et al. (2018) · The Journal of Physiology · doi:10.1113/jp275604 · Cited by 115 · see citing works
Parkin is required for exercise-induced mitophagy in muscle: Impact of aging
Chen, C. C. W., Erlich, A. T., Crilly, M. J., & Hood, D. A. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00391.2017 · Cited by 108 · see citing works
Function and Characteristics of PINK1 in Mitochondria
Matsuda, S., Kitagishi, Y., & Kobayashi, M. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/601587 · Cited by 102 · see citing works
Mitochondrial dynamics in cancer-induced cachexia
van der Ende, M., Grefte, S., Plas, R., Meijerink, J., Witkamp, R. F., Keijer, J., & van Norren, K. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.07.008 · Cited by 87 · see citing works
Haque, M. E., Mount, M. P., Safarpour, F., Abdel-Messih, E., Callaghan, S., Mazerolle, C., Kitada, T., Slack, R. S., Wallace, V., Shen, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346437 · Cited by 84 · see citing works
Loss of HtrA2/Omi activity in non-neuronal tissues of adult mice causes premature aging
Kang, S., Louboutin, J.-P., Datta, P., Landel, C. P., Martinez, D., Zervos, A. S., Strayer, D. S., Fernandes-Alnemri, T., & Alnemri, E. S. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.117 · Cited by 84 · see citing works
Kravic, B., Harbauer, A. B., Romanello, V., Simeone, L., Vögtle, F.-N., Kaiser, T., Straubinger, M., Huraskin, D., Böttcher, M., Cerqua, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1403716 · Cited by 75 · see citing works
Mitophagy is required for brown adipose tissue mitochondrial homeostasis during cold challenge
Lu, Y., Fujioka, H., Joshi, D., Li, Q., Sangwung, P., Hsieh, P., Zhu, J., Torio, J., Sweet, D., Wang, L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26394-5 · Cited by 76 · see citing works
The lifecycle of skeletal muscle mitochondria in obesity
Pileggi, C. A., Parmar, G., & Harper, M. (2021) · Obesity Reviews · doi:10.1111/obr.13164 · Cited by 61 · see citing works
The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial complex I subunit
Zhang, K., Li, Z., Jaiswal, M., Bayat, V., Xiong, B., Sandoval, H., Charng, W.-L., David, G., Haueter, C., Yamamoto, S., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201208033 · Cited by 58 · see citing works
Novel Insights into the Anti-Aging Role of Mitophagy
(2018) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2018.05.005 · Cited by 56 · see citing works
Parkin Overexpression Attenuates Sepsis-Induced Muscle Wasting
Leduc-Gaudet, J.-P., Mayaki, D., Reynaud, O., Broering, F. E., Chaffer, T. J., Hussain, S. N. A., & Gouspillou, G. (2020) · Cells · doi:10.3390/cells9061454 · Cited by 54 · see citing works
Jankauskas, S. S., Pevzner, I. B., Andrianova, N. V., Zorova, L. D., Popkov, V. A., Silachev, D. N., Kolosova, N. G., Plotnikov, E. Y., & Zorov, D. B. (2017) · Scientific Reports · doi:10.1038/srep44430 · Cited by 41 · see citing works
Mitochondrial Proteolysis and Metabolic Control
Ahola, S., Langer, T., & MacVicar, T. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033936 · Cited by 37 · see citing works
A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling
Shiba-Fukushima, K., Inoshita, T., Sano, O., Iwata, H., Ishikawa, K.-I., Okano, H., Akamatsu, W., Imai, Y., & Hattori, N. (2020) · iScience · doi:10.1016/j.isci.2020.101048 · Cited by 37 · see citing works
Cheng, K. Y.-K., Bao, Z., Long, Y., Liu, C., Huang, T., Cui, C., Chow, S. K.-H., Wong, R. M. Y., & Cheung, W.-H. (2023) · Subcellular Biochemistry · doi:10.1007/978-3-031-26576-1_6 · Cited by 14 · see citing works
Shin, Y. S., Ryall, J. G., Britto, J. M., Lau, C. L., Devenish, R. J., Nagley, P., & Beart, P. M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14667 · Cited by 13 · see citing works
miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A
Markham, B. N., Ramnarine, C., Kim, S., Grever, W. E., Soto-Beasley, A. I., Heckman, M. G., Ren, Y., Osborne, A. C., Kehili, M., Bhagwate, A. V., et al. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00029-w
Self-citation
- Authors
- Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Youle, Richard J.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-11-29
- Volume
- 191
- Issue
- 5
- Pages
- 933-942
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2995166
- OpenAlex
- W2038834667
- Cited by
- 1,375
- References
- 34
- Citations by year
- 2026: 89 · 2025: 88 · 2024: 108 · 2023: 92 · 2022: 93 · 2021: 129 · 2020: 116 · 2019: 90 · 2018: 85 · 2017: 81 · 2016: 81 · 2015: 77 · 2014: 76 · 2013: 73 · 2012: 65
- FWCI
- 31.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- PINK1, PARL, mitochondrial membrane potential, mitochondrial protein import, protein degradation, Parkin, mitophagy, Parkinson's disease, rhomboid protease, mitochondrial outer membrane, inner mitochondrial membrane, protein stability
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, HeLa Cells, Humans, Protein Kinases, Transfection, Mitochondrial Proteins, RNA, Small Interfering, Metalloproteases, Mice, Membrane Potential, Mitochondrial
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