PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Open accessAbstract
Where Parkin Parks: Damaged mitochondria are removed from cells in a process known as mitophagy. Failure of this quality-control mechanism contributes to Parkinson's disease. When damaged mitochondria lose membrane depolarization, the protein kinase, PINK1, accumulates on the mitochondrial surface, recruits Parkin, and promotes mitophagy. Chen and Dorn (p. 471 ) describe another component of this process, mitofusin 2, which appears to function as the receptor for Parkin on the surface of damaged mitochondria.
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?
Mfn2 has been shown to participate in mitophagy in cardiomyocytes.
“Moreover, Mfn2 has been shown to participate in mitophagy in cardiomyocytes (Chen & Dorn, 2013; Song et al, 2015).”
From Mfn2 deficiency links age‐related sarcopenia and impaired autophagy to activation of an adaptive mitophagy pathway (2016) · cites this paper as Chen & Dorn, 2013
When PINK1 phosphorylates MFN2, it becomes a receptor for the ubiquitin ligase Parkin to activate mitophagy.
“For instance, when PINK1 phosphorylates MFN2, it becomes a receptor for the ubiquitin ligase Parkin to activate mitophagy [69].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [69]
Cardiomyocyte-specific deletion of Mnf2 causes progressive cardiomyopathy due to accumulation of morphologically and functionally abnormal mitochondria.
“| Cardiomyopathies | Cardiomyocyte‐specific deletion of Mnf2 | Progressive cardiomyopathy due to accumulation of morphologically and functionally abnormal mitochondria | Chen and Dorn (2013) |”
From Autophagy in major human diseases (2021) · cites this paper as Chen and Dorn (2013)
Parkin recruitment initiates localization of damaged mitochondria to LC3-containing membranes, leading to autophagosome formation.
“This initiates the localization of damaged mitochondria to membranes containing microtubule-associated protein light-chain 3 (LC3) leading to the formation of autophagosomes (20, 21).”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [21]
Once recruited to mitochondria, Parkin mediates degradation of mitofusin-2 and prevents mitochondrial fusion.
“Once recruited to mitochondria, Parkin mediates degradation of mitofusin-2 (Mfn2; a core protein involved in mitochondrial fusion) and hence prevents mitochondrial fusion.”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [21]
Autophagosomes containing damaged mitochondria fuse with lysosomes and are cleared from cells.
“These autophagosomes containing the damaged mitochondria fuse with lysosomes which are cleared from the cells (16–21).”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [21]
Once activated, Parkin facilitates ubiquitination of numerous outer mitochondrial membrane proteins, including Mfn1, Mfn2, VDAC, Tom20, and Miro.
“Once activated, Parkin has been reported to facilitate ubiquitination of numerous OMM proteins, including Mfn1 [126,127,128], Mfn2 [129], VDAC [130], Tom20 (translocase of the outer membrane 20) [121], and Miro [131].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [129]
Parkin-mediated mitophagy is proposed to be involved in cardiomyocyte development and prevents aging-related loss of muscle mass and strength.
“Parkin-mediated mitophagy is proposed to be involved in cardiomyocyte development and prevents aging-related loss of muscle mass and strength (Chen and Dorn, 2013, Leduc-Gaudet et al., 2019).”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Chen and Dorn, 2013
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
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · 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
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · 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
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993 · see citing works
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924 · see citing works
Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910 · see citing works
Sebastián, D., Hernández-Alvarez, M. I., Segalés, J., Sorianello, E., Muñoz, J. P., Sala, D., Waget, A., Liesa, M., Paz, J. C., Gopalacharyulu, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108220109 · Cited by 673 · see citing works
Schapira, A. H. V. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68970-8 · Cited by 594 · see citing works
Mitochondrial Fusion is Essential for Organelle Function and Cardiac Homeostasis
Chen, Y., Liu, Y., & Dorn, G. W. (2011) · Circulation Research · doi:10.1161/circresaha.111.258723 · Cited by 506 · see citing works
Self-citationBaloh, R., Schmidt, R., Pestronk, A., & Milbrandt, J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4798-06.2007 · Cited by 471 · see citing works
Beilina, A. G., van der Brug, M., Ahmad, R., Kesavapany, S., Miller, D. W., Petsko, G. A., & Cookson, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500617102 · Cited by 382 · see citing works
Chen, Y., Csordás, G., Jowdy, C. C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 348 · see citing works
Self-citationRegulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
Karbowski, M., & Youle, R. J. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.05.007 · Cited by 256 · see citing works
Mutations in PINK1 and Parkin Impair Ubiquitination of Mitofusins in Human Fibroblasts
Raković, A., Grünewald, A., Kottwitz, J., Brüggemann, N., Pramstaller, P. P., Lohmann, K., & Klein, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016746 · Cited by 234 · see citing works
Contribution of Impaired Mitochondrial Autophagy to Cardiac Aging
Dutta, D., Calvani, R., Bernabei, R., Leeuwenburgh, C., & Marzetti, E. (2012) · Circulation Research · doi:10.1161/circresaha.111.246108 · Cited by 221 · see citing works
Mitofusin 2 is necessary for striatal axonal projections of midbrain dopamine neurons
Lee, S., Sterky, F. H., Mourier, A., Terzioglu, M., Cullheim, S., Olson, L., & Larsson, N. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds352 · Cited by 177 · see citing works
MARF and Opa1 Control Mitochondrial and Cardiac Function in Drosophila
Dorn, G. W., Clark, C. F., Eschenbacher, W. H., Kang, M., Engelhard, J. T., Warner, S. J., Matkovich, S. J., & Jowdy, C. C. (2010) · Circulation Research · doi:10.1161/circresaha.110.236745 · Cited by 136 · see citing works
Self-citationThe Transcription Factor GATA-6 Regulates Pathological Cardiac Hypertrophy
van Berlo, J. H., Elrod, J. W., van den Hoogenhof, M. M. G., et al. (2010) · Circulation Research · doi:10.1161/circresaha.110.220764 · Cited by 108 · see citing works
Zesiewicz, T., Strom, J. A., Borenstein, A. R., et al. (2004) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2004.04.001 · Cited by 60 · see citing works
Hosokawa, T., Saito, T., Asada, A., Fukunaga, K., & Hisanaga, S. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900578-mcp200 · Cited by 57 · see citing works
Eschenbacher, W. H., Song, M., Chen, Y., Bhandari, P., Zhao, P. Y., Jowdy, C. C., Engelhard, J. T., & Dorn, G. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044296 · Cited by 29 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Hallmarks of Cellular Senescence
Hernandez-Segura, A., Nehme, J., & Demaria, M. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.001 · Cited by 2,605 · 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-citationThe 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
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works
Autophagy in major human diseases
Klionsky, D. J., Petroni, G., Amaravadi, R. K., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cadwell, K., Cecconi, F., Choi, A. M. K., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108863 · Cited by 1,585 · see citing works
Cargo recognition and trafficking in selective autophagy
Stolz, A., Ernst, A., & Dikic, I. (2014) · Nature Cell Biology · doi:10.1038/ncb2979 · Cited by 1,207 · see citing works
Cargo recognition and degradation by selective autophagy
Gatica, D., Lahiri, V., & Klionsky, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0037-z · Cited by 1,067 · 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
Wang, G., McCain, M. L., Yang, L., He, A., Pasqualini, F. S., Agarwal, A., Yuan, H., Jiang, D., Zhang, D., Zangi, L., et al. (2014) · Nature Medicine · doi:10.1038/nm.3545 · Cited by 837 · see citing works
Autophagy and mitophagy in cardiovascular disease
Bravo-San Pedro, J. M., Kroemer, G., & Galluzzi, L. (2017) · Circulation Research · doi:10.1161/circresaha.117.311082 · Cited by 843 · see citing works
Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis
Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S. (2021) · The FASEB Journal · doi:10.1096/fj.202100067r · Cited by 733 · see citing works
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions
Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625 · see citing works
The Role of Autophagy in the Heart
Sciarretta, S., Maejima, Y., Zablocki, D., & Sadoshima, J. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121427 · Cited by 547 · see citing works
Critical reappraisal confirms that Mitofusin 2 is an endoplasmic reticulum–mitochondria tether
Naon, D., Zaninello, M., Giacomello, M., Varanita, T., Grespi, F., Lakshminaranayan, S., Serafini, A., Semenzato, M., Herkenne, S., Hernández-Alvarez, M. I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606786113 · Cited by 521 · see citing works
Self-citationMitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease
Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.02.003 · Cited by 524 · 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
Song, M., Mihara, K., Chen, Y., Scorrano, L., & Dorn, G. W. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.011 · Cited by 482 · see citing works
Self-citationMitochondrial biogenesis and dynamics in the developing and diseased heart
Dorn, G. W., Vega, R. B., & Kelly, D. P. (2015) · Genes & Development · doi:10.1101/gad.269894.115 · Cited by 470 · 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
Mitochondria and ageing: Role in heart, skeletal muscle and adipose tissue
Boengler, K., Kosiol, M., Mayr, M., Schulz, R., & Rohrbach, S. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12178 · Cited by 421 · see citing works
Sebastián, D., Sorianello, E., Segalés, J., Irazoki, A., Ruiz‐Bonilla, V., Sala, D., Planet, E., Berenguer‐Llergo, A., Muñoz, J. P., Sánchez‐Feutrie, M., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593084 · Cited by 396 · 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
Wang, B., Nie, J., Wu, L., Hu, Y., Wen, Z., Dong, L., Zou, M.-H., Chen, C., & Wang, D. W. (2018) · Circulation Research · doi:10.1161/circresaha.117.312317 · Cited by 334 · see citing works
Abrogating Mitochondrial Dynamics in Mouse Hearts Accelerates Mitochondrial Senescence
Song, M., Franco, A., Fleischer, J. A., Zhang, L., & Dorn, G. W. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.09.023 · Cited by 309 · see citing works
Self-citationHow 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
Self-citationZhan, M., Usman, I. M., Sun, L., & Kanwar, Y. S. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014050457 · Cited by 288 · 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
Ahmad, T., Sundar, I. K., Lerner, C. A., Gerloff, J., Tormos, A. M., Yao, H., & Rahman, I. (2015) · The FASEB Journal · doi:10.1096/fj.14-268276 · Cited by 264 · see citing works
Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
Leduc-Gaudet, J.-P., Hussain, S. N. A., Barreiro, E., & Gouspillou, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158179 · Cited by 268 · see citing works
“To date, the modulation (overexpression or deletion) of proteins regulating mitochondrial dynamics in mice has either shown no benefit to muscle cells [68] or was proven deleterious to muscle health (Drp1 overexpression, Drp1 knockout, Drp1 knockdown, and Mfn1+Mfn2 knockout).”
BackgroundInfluentialDisease-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
Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244 · see citing works
Gorski, P. A., Ceholski, D. K., & Hajjar, R. J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.01.005 · Cited by 213 · see citing works
TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control
Gatliff, J., East, D., Crosby, J., Abeti, R., Harvey, R., Craigen, W., Parker, P., & Campanella, M. (2014) · Autophagy · doi:10.4161/15548627.2014.991665 · Cited by 215 · 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
Mitophagy-dependent macrophage reprogramming protects against kidney fibrosis
Bhatia, D., Chung, K.-P., Nakahira, K., Patino, E., Rice, M. C., Torres, L. K., Muthukumar, T., Choi, A. M. K., Akchurin, O. M., & Choi, M. E. (2019) · JCI Insight · doi:10.1172/jci.insight.132826 · Cited by 185 · 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
Autophagy in hepatic adaptation to stress
Hazari, Y., Bravo-San Pedro, J. M., Hetz, C., Galluzzi, L., & Kroemer, G. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2019.08.026 · Cited by 151 · see citing works
Neuronal mitochondria transport Pink1 mRNA via synaptojanin 2 to support local mitophagy
Harbauer, A. B., Hees, J. T., Wanderoy, S., Segura, I., Gibbs, W., Cheng, Y., Ordonez, M., Cai, Z., Cartoni, R., Ashrafi, G., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.035 · Cited by 156 · see citing works
The NLRP3 Inflammasome is Involved in the Pathogenesis of Parkinson’s Disease in Rats
Mao, Z., Liu, C., Ji, S., Yang, Q., Ye, H., Han, H., & Xue, Z. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2185-0 · Cited by 155 · see citing works
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 · see citing works
“Mitofusin 2 (Mfn2) has an important role regulating mitochondrial fusion, but it also acts as a receptor for Pink1 and Parkin-targeted mitophagy (27).”
BackgroundExercise reestablishes autophagic flux and mitochondrial quality control in heart failure
Campos, J. C., Queliconi, B. B., Bozi, L. H. M., Bechara, L. R. G., Dourado, P. M. M., Andres, A. M., Jannig, P. R., Gomes, K. M. S., Zambelli, V. O., Rocha-Resende, C., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1325062 · Cited by 146 · see citing works
Carter, H. N., Kim, Y., Erlich, A. T., Zarrin‐khat, D., & Hood, D. A. (2018) · The Journal of Physiology · doi:10.1113/jp275998 · Cited by 136 · see citing works
Yeo, D., Kang, C., Gomez-Cabrera, M. C., Vina, J., & Ji, L. L. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.456 · Cited by 137 · see citing works
Mitophagy in Acute Kidney Injury and Kidney Repair
Wang, Y., Cai, J., Tang, C., & Dong, Z. (2020) · Cells · doi:10.3390/cells9020338 · Cited by 130 · 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
Mitochondrial DNA damage and atherosclerosis
Yu, E. P. K., & Bennett, M. R. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.008 · Cited by 124 · see citing works
Li, S., Lin, Q., Shao, X., Zhu, X., Wu, J., Wu, B., Zhang, M., Zhou, W., Zhou, Y., Jin, H., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.12.005 · Cited by 112 · see citing works
Parkin mutations reduce the complexity of neuronal processes in iPSC-derived human neurons
Ren, Y., Jiang, H., Hu, Z., Fan, K., Wang, J., Janoschka, S., Wang, X., Ge, S., & Feng, J. (2015) · Stem Cells · doi:10.1002/stem.1854 · Cited by 109 · 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
PINK1: The guard of mitochondria
Wang, N., Zhu, P., Huang, R., Wang, C., Sun, L., Lan, B., He, Y., Zhao, H., & Gao, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118247 · Cited by 107 · see citing works
Kubli, D. A., Cortez, M. Q., Moyzis, A. G., Najor, R. H., Lee, Y., & Gustafsson, Å. B. (2015) · PLOS ONE · doi:10.1371/journal.pone.0130707 · Cited by 102 · see citing works
Wohlgemuth, S. E., Calvani, R., & Marzetti, E. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.03.007 · Cited by 97 · see citing works
Xu, L., Wu, Z., He, Y., Chen, Z., Xu, K., Yu, W., Fang, W., Ma, C., Moqbel, S. A. A., Ran, J., et al. (2020) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2019.11.011 · Cited by 87 · see citing works
Morsci, N. S., Hall, D. H., Driscoll, M., & Sheng, Z.-H. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.2799-15.2016 · Cited by 92 · see citing works
Park, J., Choi, H., Min, J., Kim, B., Lee, S., Yun, J. W., Choi, M., Chang, K., & Lee, D. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12984 · Cited by 93 · 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
Mitochondrial dynamics: orchestrating the journey to advanced age
Biala, A. K., Dhingra, R., & Kirshenbaum, L. A. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.04.015 · Cited by 82 · see citing works
Mitochondrial function and mitochondrial DNA maintenance with advancing age
Gaziev, A. I., Abdullaev, S., & Podlutsky, A. (2014) · Biogerontology · doi:10.1007/s10522-014-9515-2 · Cited by 77 · 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
Cilenti, L., Ambivero, C. T., Ward, N., Alnemri, E. S., Germain, D., & Zervos, A. S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.027 · Cited by 70 · see citing works
Thai, P. N., Seidlmayer, L. K., Miller, C., Ferrero, M., Dorn, G. W., Schaefer, S., Bers, D. M., & Dedkova, E. N. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00382 · Cited by 66 · 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
Etiology of type 2 diabetes and Alzheimer’s disease: Exploring the mitochondria
Silzer, T. K., & Phillips, N. R. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.04.004 · Cited by 53 · see citing works
The cardioprotective compound cloxyquin uncouples mitochondria and induces autophagy
Zhang, J., Nadtochiy, S. M., Urciuoli, W. R., & Brookes, P. S. (2016) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00926.2014 · Cited by 36 · 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
- Authors
- Chen, Y., & Dorn, G. W.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Dorn, Gerald W.
- Venue
- Science
- Published
- 2013-04-26
- Volume
- 340
- Issue
- 6131
- Pages
- 471-475
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3774525
- OpenAlex
- W2086557228
- Cited by
- 1,323
- References
- 22
- Citations by year
- 2026: 51 · 2025: 85 · 2024: 101 · 2023: 97 · 2022: 119 · 2021: 128 · 2020: 117 · 2019: 98 · 2018: 112 · 2017: 89 · 2016: 89 · 2015: 89 · 2014: 97 · 2013: 47 · 2012: 1
- FWCI
- 78.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL059888, R21HL107276)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- PINK1, mitofusin 2, Parkin, mitophagy, selective autophagy, mitochondrial quality control, ubiquitination, mitochondrial depolarization, cardiomyopathy, respiratory dysfunction, Parkinson's disease
- MeSH terms
- PTEN-Induced Putative Kinase, Amino Acid Sequence, Animals, Autophagy, Drosophila melanogaster, Fibroblasts, Humans, Mice, Mutant Strains, Mitochondria, Mitochondria, Heart, Molecular Sequence Data, Cardiomyopathies, Phosphorylation, Protein Kinases, GTP Phosphohydrolases, Myocytes, Cardiac, Ubiquitin-Protein Ligases, Mice, Ubiquitination, HEK293 Cells
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
