Cited by 190Mitochondrial Function and PathologyParkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and Therapy

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission

Open access

Liu, Wencheng, Acín-Peréz, Rebeca, Geghman, Kindiya D., Manfredi, Giovanni, Lu, Bingwei, Li, Chenjian·2011·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1107332108PMC PMC3150934

Open this paper in CoChat — free account Open PDF

Abstract

Mutations in PTEN-induced kinase 1 (PINK1), a mitochondrial Ser/Thr kinase, cause an autosomal recessive form of Parkinson's disease (PD), PARK6. To investigate the mechanism of PINK1 pathogenesis, we used the Drosophila Pink1 knockout (KO) model. In mitochondria isolated from Pink1-KO flies, mitochondrial respiration driven by the electron transport chain (ETC) is significantly reduced. This reduction is the result of a decrease in ETC complex I and IV enzymatic activity. As a consequence, Pink1-KO flies also display a reduced mitochondrial ATP synthesis. Because mitochondrial dynamics is important for mitochondrial function and Pink1-KO flies have defects in mitochondrial fission, we explored whether fission machinery deficits underlie the bioenergetic defect in Pink1-KO flies. We found that the bioenergetic defects in the Pink1-KO can be ameliorated by expression of Drp1, a key molecule in mitochondrial fission. Further investigation of the ETC complex integrity in wild type, Pink1-KO, PInk1-KO/Drp1 transgenic, or Drp1 transgenic flies indicates that the reduced ETC complex activity is likely derived from a defect in the ETC complex assembly, which can be partially rescued by increasing mitochondrial fission. Taken together, these results suggest a unique pathogenic mechanism of PINK1 PD: The loss of PINK1 impairs mitochondrial fission, which causes defective assembly of the ETC complexes, leading to abnormal bioenergetics.

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

Crossref · 10.1073/pnas.1107332108

Cites

47 of 47 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Parkinson's Disease
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
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
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
PINK1/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
Mitochondrial Complex I Deficiency in Parkinson's Disease
Schapira, A. H. V., Cooper, J. M., Dexter, D., Clark, J. B., Jenner, P., & Marsden, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb02325.x · Cited by 2,283
Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
Schägger, H., & von JAGOW, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90094-a · Cited by 2,267
Mitochondria: Dynamic Organelles in Disease, Aging, and Development
Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869

Show all 47 references

Sorted by citations

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
Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease
Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357
Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.
Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274
Mitochondrial Dynamics — Mitochondrial Fission and Fusion in Human Diseases
Archer, S. L. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1215233 · Cited by 1,120
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
PINK1 deficiency impairs mitochondrial homeostasis and promotes lung fibrosis
Bueno, M., Lai, Y.-C., Romero, Y., Brands, J., St. Croix, C. M., Kamga, C., Corey, C., Herazo-Maya, J. D., Sembrat, J., Lee, J. S., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci74942 · Cited by 627
The aging lung: Physiology, disease, and immunity
Schneider, J. L., Rowe, J. H., Garcia-de-Alba, C., Kim, C. F., Sharpe, A. H., & Haigis, M. C. (2021) · Cell · doi:10.1016/j.cell.2021.03.005 · Cited by 500
Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner
Frank, M., Duvezin-Caubet, S., Koob, S., Occhipinti, A., Jagasia, R., Petcherski, A., Ruonala, M. O., Priault, M., Salin, B., & Reichert, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.08.007 · Cited by 468
The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity
Wang, W., Wang, L., Lu, J., Siedlak, S. L., Fujioka, H., Liang, J., Jiang, S., Ma, X., Jiang, Z., da Rocha, E. L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4130 · Cited by 480
Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology
Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 401
Parkinson's Disease–Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria
Liu, S., Sawada, T., Lee, S., Yu, W., Silverio, G., Alapatt, P., Millan, I., Shen, A., Saxton, W., Kanao, T., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002537 · Cited by 371
Self-citation
PINK1 Loss-of-Function Mutations Affect Mitochondrial Complex I Activity via NdufA10 Ubiquinone Uncoupling
Morais, V. A., Haddad, D., Craessaerts, K., Bock, P. D., Swerts, J., Vilain, S., Aerts, L., Overbergh, L., Grünewald, A., Seibler, P., et al. (2014) · Science · doi:10.1126/science.1249161 · Cited by 373
The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons
Wang, W., Li, L., Lin, W.-L., Dickson, D. W., Petrucelli, L., Zhang, T., & Wang, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt319 · Cited by 367
BNIP3 Protein Suppresses PINK1 Kinase Proteolytic Cleavage to Promote Mitophagy
Zhang, T., Xue, L., Li, L., Tang, C., Wan, Z., Wang, R., Tan, J., Tan, Y., Han, H., Tian, R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733410 · Cited by 293
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250
Inhibition of mitophagy drives macrophage activation and antibacterial defense during sepsis
Patoli, D., Mignotte, F., Deckert, V., Dusuel, A., Dumont, A., Rieu, A., Jalil, A., Dongen, K. V., Bourgeois, T., Gautier, T., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci130996 · Cited by 251
Abnormal Mitochondrial Dynamics in the Pathogenesis of Alzheimer's Disease
Zhu, X., Perry, G., Smith, M. A., & Wang, X. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-129005 · Cited by 242
Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation
Su, Y.-C., & Qi, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt301 · Cited by 233
Alterations in Mitochondrial Quality Control in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 226
PINK1 and Parkin Control Localized Translation of Respiratory Chain Component mRNAs on Mitochondria Outer Membrane
Gehrke, S., Wu, Z., Klinkenberg, M., Sun, Y., Auburger, G. W. J., Guo, S., & Lu, B. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.007 · Cited by 223
Self-citation
Mitochondrial dynamics and transport in Alzheimer's disease
Flannery, P. J., & Trushina, E. V. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.06.009 · Cited by 203
Antioxidant gene therapy against neuronal cell death
Navarro-Yepes, J., Zavala-Flores, L. M., Anandhan, A., Wang, F., Skotak, M., Chandra, N., Li, M., Pappa, A., Martínez‐Fong, D., Razo, L. M. D., et al. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.007 · Cited by 182
Inhibition of mitochondrial fragmentation protects against Alzheimer’s disease in rodent model
Wang, W., Yin, J., Ma, X., Zhao, F., Siedlak, S. L., Wang, Z., Torres, S., Fujioka, H., Xu, Y., Perry, G., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx299 · Cited by 175
Antiaging properties of a grape-derived antioxidant are regulated by mitochondrial balance of fusion and fission leading to mitophagy triggered by a signaling network of Sirt1-Sirt3-Foxo3-PINK1-PARKIN
Das, S., Mitrovsky, G., Vasanthi, H. R., & Das, D. K. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/345105 · Cited by 173
Retracted
A Small Molecule Promotes Mitochondrial Fusion in Mammalian Cells
Wang, D., Wang, J., Bonamy, G. M. C., Meeusen, S., Brusch, R. G., Turk, C. N., Yang, P., & Schultz, P. G. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204589 · Cited by 165
The role of mitochondrial DNA mutation on neurodegenerative diseases
Cha, M.-Y., Kim, D. K., & Mook‐Jung, I. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.122 · Cited by 157
Inhibition of Drp1 mitochondrial translocation provides neural protection in dopaminergic system in a Parkinson’s disease model induced by MPTP
Filichia, E., Hoffer, B. J., Qi, X., & Luo, Y. (2016) · Scientific Reports · doi:10.1038/srep32656 · Cited by 157
Mitochondria initiate and regulate sarcopenia
Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153
“However, mitochondrial damage and modifications also may occur by posttranslational modifications such as ubiquitination (67,99,140,148), acetylation (9,21,28), succinylation (114,150), and phosphorylation (51,73,79).”
Background
Cyanidin‐3‐O‐glucoside improves non‐alcoholic fatty liver disease by promoting PINK1‐mediated mitophagy in mice
Li, X., Shi, Z., Zhu, Y., Shen, T., Wang, H., Shui, G., Loor, J. J., Fang, Z., Chen, M., Wang, X., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15083 · Cited by 153
A Mitocentric View of Parkinson's Disease
Haelterman, N. A. T., Yoon, W. H., Sandoval, H., Jaiswal, M., Shulman, J. M., & Bellen, H. J. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014317 · Cited by 141
Mitochondrial Respiratory Chain Supercomplexes: From Structure to Function
Guan, S., Zhao, L., & Peng, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213880 · Cited by 151
A review of genome‐wide transcriptomics studies in Parkinson's disease
Borrageiro, G., Haylett, W. L., Seedat, S., Kuivaniemi, H., & Bardien, S. (2017) · European Journal of Neuroscience · doi:10.1111/ejn.13760 · Cited by 111
PINK1-mediated mitophagy protects against hepatic ischemia/reperfusion injury by restraining NLRP3 inflammasome activation
Xu, Y., Tang, Y., Lu, J., Zhang, W., Zhu, Y., Zhang, S., Ma, G., Jiang, P., & Zhang, W. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.015 · Cited by 113
Mitochondrial Dynamics: The Intersection of Form and Function
Ferree, A. W., & Shirihai, O. S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_2 · Cited by 113
PINK1-mediated Drp1S616 phosphorylation modulates synaptic development and plasticity via promoting mitochondrial fission
Gao, Q., Tian, R., Han, H., Slone, J. D., Wang, C., Ke, X., Zhang, T., Li, X., He, Y., Liao, P., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00933-z · Cited by 119
Drosophila as a Model to Study Mitochondrial Dysfunction in Parkinson's DiseasePreprint
Guo, M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009944 · Cited by 111
Mfn2 ablation causes an oxidative stress response and eventual neuronal death in the hippocampus and cortex
Jiang, S., Nandy, P., Wang, W., Ma, X., Hsia, J., Wang, C., Wang, Z., Niu, M., Siedlak, S. L., Torres, S. L., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0238-8 · Cited by 104
MFN2 couples glutamate excitotoxicity and mitochondrial dysfunction in motor neurons
Wang, W., Zhang, F., Li, L., Tang, F., Siedlak, S. L., Fujioka, H., Liu, Y., Su, B., Pi, Y., & Wang, X. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.617167 · Cited by 103
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
Role of Dynamin-Related Protein 1 (Drp1)-Mediated Mitochondrial Fission in Oxygen Sensing and Constriction of the Ductus Arteriosus
Hong, Z., Kutty, S., Tóth, P. T., Marsboom, G., Hammel, J. M., Chamberlain, C., Ryan, J. J., Zhang, H. J., Sharp, W. W., Morrow, E., et al. (2013) · Circulation Research · doi:10.1161/circresaha.111.300285 · Cited by 100
The mitochondrial kinase PINK 1: functions beyond mitophagy
Voigt, A., Berlemann, L. A., & Winklhofer, K. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13655 · Cited by 100
Mechanisms of Parkinson's Disease
Hewitt, V. L., & Whitworth, A. J. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.005 · Cited by 97
Probing Mechanisms That Underlie Human Neurodegenerative Diseases in Drosophila
Jaiswal, M., Sandoval, H., Zhang, K., Bayat, V., & Bellen, H. J. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155456 · Cited by 100
Genes associated with Parkinson's disease: regulation of autophagy and beyond
Beilina, A. G., & Cookson, M. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13266 · Cited by 98
Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links Co-translational Quality Control to PINK1-Directed Mitophagy
Wu, Z., Wang, Y., Lim, J., Liu, B., Li, Y., Vartak, R. S., Stankiewicz, T. R., Montgomery, S. B., & Lu, B. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.007 · Cited by 87
Self-citation
Ret rescues mitochondrial morphology and muscle degeneration of Drosophila Pink1 mutants
Klein, P., Müller-Rischart, A. K., Motori, E., Schönbauer, C., Schnorrer, F., Winklhofer, K. F., & Klein, R. (2014) · The EMBO Journal · doi:10.1002/embj.201284290 · Cited by 90
PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency
Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00363-x · Cited by 91
Parkinson's Disease Phenotypes in Patient Neuronal Cultures and Brain Organoids Improved by 2‐Hydroxypropyl‐β‐Cyclodextrin Treatment
Jarazo, J., Barmpa, K., Modamio, J., Saraiva, C., Sabaté‐Soler, S., Rosety, I., Griesbeck, A., Skwirblies, F., Zaffaroni, G., Smits, L. M., et al. (2021) · Movement Disorders · doi:10.1002/mds.28810 · Cited by 98
Pink1-deficiency in mice impairs gait, olfaction and serotonergic innervation of the olfactory bulb
Glasl, L., Kloos, K., Giesert, F., Röthig, A. H. J., Benedetto, B. D., Kühn, R., Zhang, J., Hafen, U., Zerle, J., Hofmann, A., et al. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.002 · Cited by 87
The Complex I Subunit NDUFA10 Selectively Rescues Drosophila pink1 Mutants through a Mechanism Independent of Mitophagy
Pogson, J. H., Ivatt, R. M., Sánchez-Martínez, Á., Tufi, R., Wilson, E. L., Mortiboys, H., & Whitworth, A. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004815 · Cited by 87
PINK1 in the limelight: multiple functions of an eclectic protein in human health and disease
Arena, G., & Valente, E. M. (2016) · The Journal of Pathology · doi:10.1002/path.4815 · Cited by 79
Aconitase Causes Iron Toxicity in Drosophila pink1 Mutants
Esposito, G., Vos, M. H., Vilain, S., Swerts, J., Valadas, J. S., Meensel, S. V., Schaap, O., & Verstreken, P. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003478 · Cited by 74
The Parkinson’s gene PINK1 regulates cell cycle progression and promotes cancer-associated phenotypes
O’Flanagan, C. H., Morais, V. A., Wurst, W., Strooper, B. D., & O’Neill, C. (2014) · Oncogene · doi:10.1038/onc.2014.81 · Cited by 78
Parkinson's disease proteins: Novel mitochondrial targets for cardioprotection
Mukherjee, U., Ong, S., Ong, S., & Hausenloy, D. J. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.10.005 · Cited by 72
Alternative oxidase rescues mitochondria-mediated dopaminergic cell loss in Drosophila
Humphrey, D. M., Parsons, R. B., Ludlow, Z. N., Riemensperger, T. D., Esposito, G., Verstreken, P., Jacobs, H. T., Birman, S., & Hirth, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds096 · Cited by 75
The multi‐faceted role of mitochondria in the pathology of Parkinson’s disease
Trinh, D., Israwi, A. R., Arathoon, L. R., Gleave, J. A., & Nash, J. E. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15154 · Cited by 74
The complicated role of mitochondria in the podocyte
Gujarati, N. A., Vasquez, J. M., Bogenhagen, D. F., & Mallipattu, S. K. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00393.2020 · Cited by 68
CircEPS15, as a sponge of MIR24-3p ameliorates neuronal damage in Parkinson disease through boosting PINK1-PRKN-mediated mitophagy
Zhou, Y., Liu, Y., Kang, Z., Yao, H. P., Song, N., Wang, M., Song, C., Zhang, K., Ding, J., Tang, J., et al. (2023) · Autophagy · doi:10.1080/15548627.2023.2196889 · Cited by 72
Mitochondrial dynamics and mitophagy in Parkinson's disease: A fly point of view
von Stockum, S., Nardin, A., Schrepfer, E., & Ziviani, E. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.11.002 · Cited by 70
SLP-2 interacts with Parkin in mitochondria and prevents mitochondrial dysfunction in Parkin-deficient human iPSC-derived neurons andDrosophila
Zanon, A., Kalvakuri, S., Raković, A., Foco, L., Guida, M., Schwienbacher, C., Serafin, A., Rudolph, F., Trilck, M., Grünewald, A., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx132 · Cited by 70
Mitochondrial dynamic abnormalities in amyotrophic lateral sclerosis
Jiang, Z., Wang, W., Perry, G., Zhu, X., & Wang, X. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0037-x · Cited by 66
Metabolic Stress and Disorders Related to Alterations in Mitochondrial Fission or Fusion.
Babbar, M., & Sheikh, M. S. (2013) · PubMed · Cited by 70
PINK1 signalling in cancer biology
O’Flanagan, C. H., & O’Neill, C. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.10.006 · Cited by 66
The Multifaceted Roles of Zinc in Neuronal Mitochondrial Dysfunction
Liu, H. Y., Gale, J. R., Reynolds, I. J., Weiss, J. H., & Aizenman, E. (2021) · Biomedicines · doi:10.3390/biomedicines9050489 · Cited by 68
Involvement and interplay of Parkin, PINK1, and DJ1 in neurodegenerative and neuroinflammatory disorders
Wilhelmus, M. M. M., Nijland, P. G., Drukarch, B., de Vries, H. E., & van Horssen, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.040 · Cited by 62
Quantitative expression proteomics and phosphoproteomics profile of brain from PINK1 knockout mice: insights into mechanisms of familial Parkinson's disease
Triplett, J. C., Zhang, Z., Sultana, R., Cai, J., Klein, J. B., Büeler, H., & Butterfield, D. A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13039 · Cited by 58
A reduction in Drp1-mediated fission compromises mitochondrial health in autosomal recessive spastic ataxia of Charlevoix Saguenay
Bradshaw, T. Y., Romano, L. E. L., Duncan, E. J., Nethisinghe, S., Abeti, R., Michael, G. J., Giunti, P., Vermeer, S., & Chapple, J. P. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw173 · Cited by 58
Mitochondrial dysfunction in Alzheimer’s disease: a key frontier for future targeted therapies
Wang, S., Liao, Z., Zhang, Q., Han, X., Liu, C., & Wang, J. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1484373 · Cited by 67
From physiology to pathology: Emerging roles of GPER in cardiovascular disease
Wang, Z., Liu, J., Chen, Y., Tang, Y., Chen, T., Zhou, C. S., Wang, S., Chang, R., Chen, Z., Yang, W., et al. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108801 · Cited by 57
Tricornered/NDR kinase signaling mediates PINK1-directed mitochondrial quality control and tissue maintenancePreprint
Wu, Z., Sawada, T., Shiba, K., Liu, S., Kanao, T., Takahashi, R., Hattori, N., Imai, Y., & Lu, B. (2013) · Genes & Development · doi:10.1101/gad.203406.112 · Cited by 59
Self-citation
Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism
Marelja, Z., Leimkühler, S., & Missirlis, F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00050 · Cited by 61
The Parkinson's disease-related genes act in mitochondrial homeostasis
Sai, Y., Zou, Z., Peng, K., & Dong, Z. (2012) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2012.06.007 · Cited by 55
Near-Infrared 808 nm Light Boosts Complex IV-Dependent Respiration and Rescues a Parkinson-Related pink1 Model
Vos, M. H., Lovisa, B., Geens, A., Morais, V. A., Wagnières, G., van den Bergh, H., Ginggen, A., Strooper, B. D., Tardy, Y., & Verstreken, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078562 · Cited by 54
Mitochondrial respiratory chain disorganization in Parkinson's disease-relevant PINK1 and DJ1 mutants
López-Fabuel, I., Martin-Martin, L., Resch-Beusher, M., Azkona, G., Sánchez‐Pernaute, R., & Bolaños, J. P. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.03.023 · Cited by 53
Mitochondrial Supercomplexes: Physiological Organization and Dysregulation in Age-Related Neurodegenerative Disorders
Novack, G. V., Galeano, P., Castaño, E. M., & Morelli, L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00600 · Cited by 52
Bcl-xL Is Necessary for Neurite Outgrowth in Hippocampal Neurons
Park, H., Licznerski, P., Alavian, K. N., Shanabrough, M., & Jonas, E. A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5570 · Cited by 48
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
Conditional deletion of Ndufs4 in dopaminergic neurons promotes Parkinson’s disease-like non-motor symptoms without loss of dopamine neurons
Choi, W., Kim, H.-W., Tronche, F., Palmiter, R. D., Storm, D. R., & Xia, Z. (2017) · Scientific Reports · doi:10.1038/srep44989 · Cited by 49
Mitoplasticity: Adaptation Biology of the Mitochondrion to the Cellular Redox State in Physiology and Carcinogenesis
José, C., Melser, S., Bénard, G., & Rossignol, R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4357 · Cited by 51
Overexpression of ryanodine receptor type 1 enhances mitochondrial fragmentation and Ca 2+ -induced ATP production in cardiac H9c2 myoblasts
O‐Uchi, J., Jhun, B. S., Hurst, S., Bisetto, S., Gross, P., Chen, M., Kettlewell, S., Park, J., Oyamada, H., Smith, G. L., et al. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00094.2013 · Cited by 42
Loss of PINK1 causes age-dependent decrease of dopamine release and mitochondrial dysfunction
Zhi, L., Qin, Q., Muqeem, T., Seifert, E. L., Liu, W., Zheng, S., Li, C., & Zhang, H. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.10.025 · Cited by 45
Self-citation
Rescue of PINK1 Protein Null-specific Mitochondrial Complex IV Deficits by Ginsenoside Re Activation of Nitric Oxide Signaling
Kim, K., Song, K., Yoon, S., Shehzad, O., Kim, Y.-S., & Son, J. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.408146 · Cited by 45
Dendritic Cells Require PINK1-Mediated Phosphorylation of BCKDE1α to Promote Fatty Acid Oxidation for Immune Function
Basit, F., & de Vries, I. J. M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02386 · Cited by 41
A conserved retromer sorting motif is essential for mitochondrial DLP1 recycling by VPS35 in Parkinson’s disease model
Wang, W., Ma, X., Zhou, L., Liu, J., & Zhu, X. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw430 · Cited by 45
A High-Content Screen Identifies TPP1 and Aurora B as Regulators of Axonal Mitochondrial Transport
Shlevkov, E., Basu, H., Bray, M., Sun, Z., Wei, W., Apaydin, K. Z., Karhohs, K. W., Chen, P.-F., Smith, J. L. M., Wiskow, O., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.035 · Cited by 39
Therapeutic strategies in Parkinson's disease: what we have learned from animal models
Valadas, J. S., Vos, M. H., & Verstreken, P. (2014) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12577 · Cited by 44
PINK1 depletion sensitizes non-small cell lung cancer to glycolytic inhibitor 3-bromopyruvate: Involvement of ROS and mitophagy
Dai, K., Radin, D. P., & Leonardi, D. (2019) · Pharmacological Reports · doi:10.1016/j.pharep.2019.08.002 · Cited by 38
Genetic reduction of mitochondrial complex I function does not lead to loss of dopamine neurons in vivo
Kim, H.-W., Choi, W.-S., Sorscher, N., Park, H. J., Tronche, F., Palmiter, R. D., & Xia, Z. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.05.008 · Cited by 41
Flies with Parkinson's disease
Vanhauwaert, R., & Verstreken, P. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.02.020 · Cited by 37
Nitric Oxide Induction of Parkin Translocation in PTEN-induced Putative Kinase 1 (PINK1) Deficiency
Han, J., Kang, M., Kim, K., Han, P., Kim, H., Ha, J., & Son, J. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624767 · Cited by 37
Parkinson Disease: Translating Insights from Molecular Mechanisms to Neuroprotection
Pirooznia, S. K., Rosenthal, L. S., Dawson, V. L., & Dawson, T. M. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000189 · Cited by 36
Beyond Mitophagy: Cytosolic PINK1 as a Messenger of Mitochondrial Health
Steer, E. K., Dail, M. K., & Chu, C. T. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6206 · Cited by 35
Inhibition of the deubiquitinase USP8 corrects a Drosophila PINK1 model of mitochondria dysfunction
von Stockum, S., Sanchez-Martinez, A., Corrà, S., Chakraborty, J., Marchesan, E., Locatello, L., Da Rè, C., Cusumano, P., Caicci, F., Ferrari, V., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900392 · Cited by 30
Astrocytic Dynamin-Like Protein 1 Regulates Neuronal Protection against Excitotoxicity in Parkinson Disease
Hoekstra, J. G., Cook, T. J., Stewart, T., Mattison, H. A., Dreisbach, M. T., Hoffer, Z. S., & Zhang, J. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.10.022 · Cited by 37
Boosting mitochondrial health to counteract neurodegeneration
Burtscher, J., Romani, M., Bernardo, G., Popa, T., Ziviani, E., Hummel, F. C., Sorrentino, V., & Millet, G. P. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102289 · Cited by 36
Harnessing the Therapeutic Potential of the Nrf2/Bach1 Signaling Pathway in Parkinson’s Disease
Ahuja, M., Kaidery, N. A., Dutta, D., Attucks, O. C., Kazakov, E. H., Gazaryan, I. G., Matsumoto, M., Igarashi, K., Sharma, S. M., & Thomas, B. (2022) · Antioxidants · doi:10.3390/antiox11091780 · Cited by 34
Loss of Pink1 modulates synaptic mitochondrial bioenergetics in the rat striatum prior to motor symptoms: concomitant complex I respiratory defects and increased complex II‐mediated respiration
Stauch, K. L., Villeneuve, L. M., Purnell, P. R., Ottemann, B. M., Emanuel, K. M., & Fox, H. S. (2016) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201600005 · Cited by 32
Pantothenate kinase 2 interacts with PINK1 to regulate mitochondrial quality control via acetyl-CoA metabolism
Huang, Y., Wan, Z., Tang, Y., Xu, J., Laboret, B., Nallamothu, S., Yang, C., Liu, B., Lu, R. O., Lu, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30178-x · Cited by 33
Self-citation
Biomechanistic insights into the roles of oxidative stress in generating complex neurological disorders
Yusuf, M., Khan, M., Robaian, M. A., & Khan, R. A. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0250 · Cited by 32
PINK1 regulates mitochondrial morphology via promoting mitochondrial fission in porcine preimplantation embryos
Niu, Y., Nie, Z., Shin, K., Zhou, W., & Cui, X. (2019) · The FASEB Journal · doi:10.1096/fj.201802473r · Cited by 30

Authors: Liu, W., Acín-Peréz, R., Geghman, K. D., Manfredi, G., Lu, B., & Li, C.
Affiliations: Cornell University (US)
Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, NY 10065; and
Stanford Medicine (US)
ORCID: Liu, Wencheng
Manfredi, Giovanni
Lu, Bingwei
Li, Chenjian
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2011-07-18
Volume: 108
Issue: 31
Pages: 12920-12924
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1107332108
PMC: PMC3150934
OpenAlex: W2026648000
Cited by: 190
References: 47
Citations by year: 2026: 3 · 2025: 4 · 2024: 7 · 2023: 11 · 2022: 14 · 2021: 14 · 2020: 27 · 2019: 9 · 2018: 11 · 2017: 10 · 2016: 13 · 2015: 13 · 2014: 13 · 2013: 21 · 2012: 20
FWCI: 7.02
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Neurological Disorders and Stroke (R01NS054773)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR054926)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: PINK1, Parkinson's disease, PARK6, mitochondrial fission, Drp1, mitochondrial dynamics, electron transport chain, complex I, cytochrome c oxidase, oxidative phosphorylation, mitochondrial bioenergetics, Drosophila model, mitochondrial respiration, ATP production
MeSH terms: PTEN-Induced Putative Kinase, Adenosine Triphosphate, Animals, Electron Transport Complex IV, Cytoskeletal Proteins, Disease Models, Animal, Drosophila melanogaster, Electron Transport, Humans, Mitochondria, Mutation, Oxidative Phosphorylation, Oxygen Consumption, Parkinson Disease, Blotting, Western, Protein Serine-Threonine Kinases, GTP-Binding Proteins, Drosophila Proteins, Animals, Genetically Modified, Electron Transport Complex I, Gene Knockout Techniques

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

Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks