Mitochondrial quality control by the Pink1/Parkin system
Abstract
Mitochondrial dysfunction represents a prominent pathological feature in many neurodegenerative diseases, particularly in Parkinson's disease (PD). Mutations in the genes encoding the proteins Pink1 and Parkin have been identified as genetic risk factors in familiar cases of PD. Research during the last decade has identified both proteins as crucial components of an organellar quality control system that contributes to the maintenance of mitochondrial function in healthy cells. The Pink1/Parkin system acts as a sensor for mitochondrial quality and is activated, in particular, after the loss of the electric potential across the inner mitochondrial membrane. Pink1 molecules accumulate at the surface of damaged mitochondria to recruit and activate Parkin, which, in turn, elicits a signaling pathway eventually leading to the autophagic removal of the damaged organelles. This review summarizes recent advances in our knowledge of the functional role of the Pink1/Parkin system in preventing the accumulation of damaged mitochondria by mitophagy.
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Axonal autophagy is dependent on specialized enzymatic apparatuses, including the PINK1-PRKN complex for localized mitophagy, KIF1A/UNC-104 for autophagosome formation at the synapse, and the HTT-HAP1 complex and MAPK8IP1/JIP1 for retrograde transport of autophagosomes.
“Axonal autophagy is dependent on specialized enzymatic apparatuses, including the PINK1-PRKN complex for localized mitophagy [24], KIF1A/UNC-104 for autophagosome formation at the synapse [22,25], and the HTT-HAP1 complex and MAPK8IP1/JIP1 for retrograde transport of autophagosomes [23,26].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [24]
Cites
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
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · 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
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Hereditary 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
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
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 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · see citing works
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614 · see citing works
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · 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
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
The pathways of mitophagy for quality control and clearance of mitochondria
Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900 · 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
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477 · see citing works
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works
Genetics of Parkinson's DiseasePreprint
Klein, C., & Westenberger, A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a008888 · Cited by 1,370 · see citing works
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369 · see citing works
PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323 · 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
PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,161 · see citing works
Proteolysis: from the lysosome to ubiquitin and the proteasome
Ciechanover, A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1552 · Cited by 1,133 · see citing works
Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
Sarraf, S. A., Raman, M., Guarani, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,020 · see citing works
Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · see citing works
NIX is required for programmed mitochondrial clearance during reticulocyte maturation
Schweers, R. L., Zhang, J., Randall, M. S., Loyd, M. R., Li, W., Dorsey, F. C., Kundu, M., Opferman, J. T., Cleveland, J. L., Miller, J. L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708818104 · Cited by 939 · see citing works
Mitochondrial dynamics and mitochondrial quality control
Ni, H.-M., Williams, J. A., & Ding, W.-X. (2015) · Redox Biology · doi:10.1016/j.redox.2014.11.006 · Cited by 931 · 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
Mitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy
Okamoto, K., Kondo‐Okamoto, N., & Ohsumi, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.013 · Cited by 867 · see citing works
The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855 · see citing works
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812 · see citing works
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806 · see citing works
Mitonuclear communication in homeostasis and stress
Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787 · see citing works
<i>Drosophila</i> Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
Ziviani, E., Tao, R. N., & Whitworth, A. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913485107 · Cited by 735 · 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 · cited 6× · see citing works
“Importantly, in assigning a distinct function to the processed Pink1 species, the proposed model challenges the idea that Pink1-PF is merely a degradation intermediate (Greene et al. 2012).”
BackgroundInfluentialLoss 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
Ordureau, A., Sarraf, S. A., Duda, D. M., Heo, J., Jedrychowski, M. P., Sviderskiy, V. O., Olszewski, J. L., Koerber, J. T., Xie, T., Beausoleil, S. A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.007 · Cited by 693 · see citing works
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works
Lazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670 · see citing works
Glater, E. E., Megeath, L. J., Stowers, R. S., & Schwarz, T. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601067 · Cited by 667 · see citing works
Okatsu, K., Oka, T., Iguchi, M., Imamura, K., Kosako, H., Tani, N., Kimura, M., Go, E., Koyano, F., Funayama, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms2016 · Cited by 602 · 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
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 · cited 2× · see citing works
“Pink1-mediated phosphorylation and activation of the E3 protein-ubiquitin ligase Parkin have been the focus of extensive research (Kondapalli et al. 2012; Shiba-Fukushima et al. 2012).”
BackgroundUBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
Wenzel, D. M., Lissounov, A., Brzović, P. S., & Klevit, R. E. (2011) · Nature · doi:10.1038/nature09966 · Cited by 560 · see citing works
Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
Trempe, J.-F., Sauvé, V., Grenier, K., Seirafi, M., Tang, M. Y. H., Ménade, M., Al-Abdul-Wahid, S., Krett, J. D., Wong, K. T. K., Kozlov, G., et al. (2013) · Science · doi:10.1126/science.1237908 · Cited by 549 · see citing works
Ubiquitin: Same Molecule, Different Degradation Pathways
Clague, M. J., & Urbé, S. (2010) · Cell · doi:10.1016/j.cell.2010.11.012 · Cited by 535 · see citing works
Loss-of-Function of Human PINK1 Results in Mitochondrial Pathology and Can Be Rescued by Parkin
Exner, N., Treske, B., Paquet, D., Holmström, K. M., Schiesling, C., Gispert, S., Carballo‐Carbajal, I., Berg, D., Hoepken, H.-H., Gasser, T., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0719-07.2007 · Cited by 511 · see citing works
Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1
Kamp, F., Exner, N., Lutz, A., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 505 · see citing works
Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502 · see citing works
PINK1 cleavage at position A103 by the mitochondrial protease PARL
Deas, E., Plun‐Favreau, H., Gandhi, S., Desmond, H., Kjaer, S., Loh, S. H. Y., Renton, A. E., Harvey, R. J., Whitworth, A. J., Martins, L. M., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq526 · Cited by 501 · see citing works
The mitochondrial UPR – protecting organelle protein homeostasis
Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · 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
Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation*
Lutz, A., Exner, N., Fett, M. E., Schlehe, J. S., Kloos, K., Lämmermann, K., Brunner, B., Kurz-Drexler, A., Vogel, F., Reichert, A., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035774 · 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
Mitochondria removal by autophagy
Wang, K., & Klionsky, D. J. (2011) · Autophagy · doi:10.4161/auto.7.3.14502 · Cited by 407 · see citing works
Gispert, S., Ricciardi, F., Kurz, A., Azizov, M., Hoepken, H.-H., Becker, D., Voos, W., Leuner, K., Müller, W. E., Kudin, A. P., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005777 · Cited by 382 · see citing works
Self-citationStructure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
Riley, B. E., Lougheed, J. C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T. A., Walker, D., Yang, Y., Regnström, K. J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2982 · Cited by 368 · see citing works
Structure of the human Parkin ligase domain in an autoinhibited state
Wauer, T., & Komander, D. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.125 · Cited by 334 · see citing works
PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons
Wood-Kaczmar, A., Gandhi, S., Yao, Z., Abramov, A. S. Y., Miljan, E. A., Keen, G., Stanyer, L., Hargreaves, I., Klupsch, K., Deas, E., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002455 · Cited by 316 · 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
The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations
Geisler, S., Holmström, K. M., Treis, A., Skujat, D., Weber, S. S., Fiesel, F. C., Kahle, P. J., & Springer, W. (2010) · Autophagy · doi:10.4161/auto.6.7.13286 · Cited by 311 · cited 3× · see citing works
“Providing an explanation for their genetic interaction, Pink1 was finally demonstrated to be responsible for Parkin translocation to depolarized mitochondria (Geisler et al. 2010b; Narendra et al. 2010; Vives-Bauza et al. 2010; Ziviani et al. 2010).”
BackgroundCharacterization 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
The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy
Rawet-Slobodkin, M., & Elazar, Z. (2013) · Essays in Biochemistry · doi:10.1042/bse0550051 · Cited by 259 · see citing works
Chaperone–protease networks in mitochondrial protein homeostasis
Voos, W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.06.005 · Cited by 221 · see citing works
Self-citationLUBAC synthesizes linear ubiquitin chains via a thioester intermediate
Stieglitz, B., Morris-Davies, A. C., Koliopoulos, M. G., Christodoulou, E., & Rittinger, K. (2012) · EMBO Reports · doi:10.1038/embor.2012.105 · Cited by 220 · see citing works
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 213 · see citing works
Smit, J. J., Monteferrario, D., Noordermeer, S. M., van Dijk, W. J., van der Reijden, B. A., & Sixma, T. K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.217 · Cited by 210 · see citing works
NBR1 co-operates with p62 in selective autophagy of ubiquitinated targets
Kirkin, V., Lamark, T., Johansen, T., & Đikić, I. (2009) · Autophagy · doi:10.4161/auto.5.5.8566 · Cited by 210 · see citing works
Mitochondrial dysfunction, peroxidation damage and changes in glutathione metabolism in PARK6
Hoepken, H.-H., Gispert, S., Morales, B., Wingerter, O., Turco, D. D., Mülsch, A., Nussbaum, R. L., Müller, K., Dröse, S., Brandt, U., et al. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.10.007 · Cited by 202 · see citing works
Pink1 disables the anti-fission machinery to segregate damaged mitochondria for mitophagy
Pryde, K. R., Smith, H. L., Chau, K.-Y., & Schapira, A. H. V. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201509003 · Cited by 185 · see citing works
NRF2 Regulates PINK1 Expression under Oxidative Stress Conditions
Murata, H., Takamatsu, H., Liu, S., Kataoka, K., Huh, N.-H., & Sakaguchi, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142438 · Cited by 183 · see citing works
Mei, Y., Zhang, Y., Yamamoto, K., Xie, W., Mak, T. W., & You, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901104106 · Cited by 172 · 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
Unlocking the presequence import pathway
Schulz, C., Schendzielorz, A. B., & Rehling, P. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.001 · Cited by 170 · see citing works
Parkin and mitochondrial quality control: toward assembling the puzzle
Winklhofer, K. F. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.01.001 · Cited by 149 · see citing works
The molecular mechanism of mitochondria autophagy in yeast
Kanki, T., & Klionsky, D. J. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.07035.x · Cited by 142 · see citing works
Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection
Trempe, J., & Fon, E. A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00038 · Cited by 130 · see citing works
PINK1-Parkin Pathway Activity Is Regulated by Degradation of PINK1 in the Mitochondrial Matrix
Thomas, R. E., Andrews, L. A., Burman, J. L., Lin, W.-Y., & Pallanck, L. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004279 · Cited by 129 · see citing works
Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy
Fedorowicz, M. A., de Vries, R. L. A., Rüb, C., Becker, D., Huang, Y., Zhou, C., Wolken, D. M. A., Voos, W., Liu, Y., & Przedborski, S. (2013) · EMBO Reports · doi:10.1002/embr.201337294 · Cited by 127 · see citing works
Self-citationParkin- and PINK1-Dependent Mitophagy in Neurons: Will the Real Pathway Please Stand Up?
Grenier, K., McLelland, G., & Fon, E. A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00100 · Cited by 120 · 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
PINK1 Kinase Catalytic Activity Is Regulated by Phosphorylation on Serines 228 and 402
Aerts, L., Craessaerts, K., Strooper, B. D., & Morais, V. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620906 · Cited by 117 · see citing works
Autophagy machinery in the context of mammalian mitophagy
Yoshii, S. R., & Mizushima, N. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.013 · Cited by 90 · see citing works
Becker, D., Richter, J., Tocilescu, M. A., Przedborski, S., & Voos, W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365700 · Cited by 77 · see citing works
Self-citationMitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expression
Gómez‐Sánchez, R., Gegg, M. E., Pedro, J. M. B., Niso‐Santano, M., Alvarez‐Erviti, L., Pizarro‐Estrella, E., Gutiérrez-Martı́n, Y., Alvarez, A. M., Fuentes, J. M., González‐Polo, R. A., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.10.021 · Cited by 57 · see citing works
NBR1 is dispensable for PARK2-mediated mitophagy regardless of the presence or absence of SQSTM1
Shi, J., Fung, G., Deng, H., Zhang, J.-Q., Fiesel, F. C., Springer, W., Li, X. X., & Luo, H. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.278 · Cited by 45 · see citing works
Restriction of trophic factors and nutrients induces PARKIN expression
Klinkenberg, M., Gispert, S., Dominguez-Bautista, J. A., Braun, I., Auburger, G., & Jendrach, M. (2012) · neurogenetics · doi:10.1007/s10048-011-0303-8 · Cited by 42 · see citing works
Oxidative Stress and Regulation of Pink1 in Zebrafish (Danio rerio)
Priyadarshini, M., Orosco, L. A., & Panula, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081851 · Cited by 32 · see citing works
Upregulation of human PINK1 gene expression by NFκB signalling
Duan, X., Tong, J., Xu, Q., Wu, Y., Cai, F., Li, T., & Song, W. (2014) · Molecular Brain · doi:10.1186/s13041-014-0057-y · Cited by 28 · see citing works
Sakurai, M., Kawamura, T., Nishimura, H., Suzuki, H., Tezuka, F., & Abe, K. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2008.167 · Cited by 24 · see citing works
Pink1, the first ubiquitin kinase
Zheng, X., & Hunter, T. R. (2014) · The EMBO Journal · doi:10.15252/embj.201489185 · Cited by 21 · see citing works
Biochemical properties of the kinase PINK1 as sensor protein for mitochondrial damage signalling
Rüb, C., Schröder, N., & Voos, W. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150005 · Cited by 9 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
“nates mitochondrial surface proteins [24].”
BackgroundChen, K., Dai, H., Yuan, J., Chen, J., Lin, L., Zhang, W., Wang, L., Zhang, J., Li, K., & He, Y. (2018) · Cell Death & Disease · doi:10.1038/s41419-017-0127-z · Cited by 150 · 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
The Role of Mitophagy in Regulating Cell Death
Li, S., Zhang, J., Liu, C., Wang, Q., Yan, J., Hui, L., Jia, Q., Shan, H., Tao, L., & Zhang, M. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6617256 · Cited by 76 · see citing works
Vincow, E. S., Thomas, R. E., Merrihew, G. E., Shulman, N. J., Bammler, T. K., MacDonald, J. W., MacCoss, M. J., & Pallanck, L. J. (2019) · Autophagy · doi:10.1080/15548627.2019.1586258 · Cited by 54 · see citing works
Role of Autophagy in Skin Photoaging: A Narrative Review
Zhong, X., Deng, Y., Yang, H., Du, X., Liu, P., & Du, Y. (2024) · Medicine · doi:10.1097/md.0000000000037178 · Cited by 18 · see citing works
- Authors
- Rüb, C., Wilkening, A., & Voos, W.
- Affiliations
- University of Bonn (DE)
- Corresponding author
- Voos, Wolfgang
- ORCID
- Voos, Wolfgang
- Venue
- Cell and Tissue Research
- Published
- 2016-09-02
- Volume
- 367
- Issue
- 1
- Pages
- 111-123
- ISSN
- 0302-766X (ISSN-L)
- 1432-0878
- OpenAlex
- W2508478749
- Cited by
- 132
- References
- 95
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 17 · 2023: 15 · 2022: 17 · 2021: 14 · 2020: 13 · 2019: 15 · 2018: 10 · 2017: 7 · 2016: 2
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell and Tissue Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (VO657/5-2)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- PINK1, Parkin, mitochondrial quality control, mitophagy, Parkinson's disease, mitochondrial dysfunction, neurodegenerative diseases, mitochondrial membrane potential, autophagy, genetic risk factors
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Humans, Mitochondria, Models, Biological, Protein Kinases, Signal Transduction, Ubiquitin-Protein Ligases, Mitophagy
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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.
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