Autophagy accounts for approximately one-third of mitochondrial protein turnover and is protein selective
Open accessAbstract
The destruction of mitochondria through macroautophagy (autophagy) has been recognised as a major route of mitochondrial protein degradation since its discovery more than 50 years ago, but fundamental questions remain unanswered. First, how much mitochondrial protein turnover occurs through auto-phagy? Mitochondrial proteins are also degraded by nonautophagic mechanisms, and the proportion of mitochondrial protein turnover that occurs through autophagy is still unknown. Second, does auto-phagy degrade mitochondrial proteins uniformly or selectively? Autophagy was originally thought to degrade all mitochondrial proteins at the same rate, but recent work suggests that mitochondrial autophagy may be protein selective. To investigate these questions, we used a proteomics-based approach in the fruit fly Drosophila melanogaster, comparing mitochondrial protein turnover rates in autophagy-deficient Atg7 mutants and controls. We found that ~35% of mitochondrial protein turnover occurred via autophagy. Similar analyses using parkin mutants revealed that parkin-dependent mitophagy accounted for ~25% of mitochondrial protein turnover, suggesting that most mitochondrial autophagy specifically eliminates dysfunctional mitochondria. We also found that our results were incompatible with uniform autophagic turnover of mitochondrial proteins and consistent with protein-selective autophagy. In particular, the autophagic turnover rates of individual mitochondrial proteins varied widely, and only a small amount of the variation could be attributed to tissue differences in mitochondrial composition and autophagy rate. Furthermore, analyses comparing autophagy-deficient and control human fibroblasts revealed diverse autophagy-dependent turnover rates even in homogeneous cells. In summary, our work indicates that autophagy acts selectively on mitochondrial proteins, and that most mitochondrial protein turnover occurs through non-autophagic processes.Abbreviations: Atg5: Autophagy-related 5 (Drosophila); ATG5: autophagy related 5 (human); Atg7: Autophagy-related 7 (Drosophila); ATG7: autophagy related 7 (human); DNA: deoxyribonucleic acid; ER: endoplasmic reticulum; GFP: green fluorescent protein; MS: mass spectrometry; park: parkin (Drosophila); Pink1: PTEN-induced putative kinase 1 (Drosophila); PINK1: PTEN-induced kinase 1 (human); PRKN: parkin RBR E3 ubiquitin protein ligase (human); RNA: ribonucleic acid; SD: standard deviation; Ub: ubiquitin/ubiquitinated; WT: wild-type; YME1L: YME1 like ATPase (Drosophila); YME1L1: YME1 like 1 ATPase (human)
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Most mitochondrial protein turnover (about 70%) occurs through non-autophagic degradative processes like mitochondrial proteases, the ubiquitin-proteasome system, and mitochondrial-derived vesicles, while mitophagy contributes the remaining one third.
“A recent proteomic study in Drosophila fibroblasts identified that most of the mitochondrial protein turnover (70% circa) occurs through the combination of non-autophagic degradative processes like mitochondrial proteases, the ubiquitin–proteasome system, and mitochondrial-derived vesicles; while the contribution of mitophagy to protein turnover is of the remaining one third [36].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [36]
Approximately 70% of mitochondrial protein turnover occurs through non-autophagic degradation processes such as mitoproteases and UPS, while autophagy accounts for about 30% of mitochondrial protein turnover.
“A recent proteomics-based study of Drosophila fibroblasts found that approximately 70% of mitochondrial protein turnover occurs through non-autophagic degradation processes such as mitoproteases and UPS; Autophagy accounts for about 30% of mitochondrial protein turnover (54).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [54]
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Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482 · see citing works
limma powers differential expression analyses for RNA-sequencing and microarray studies
Ritchie, M. E., Phipson, B., Wu, D., Hu, Y., Law, C. W., Shi, W., & Smyth, G. K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv007 · Cited by 40,458 · see citing works
BLAST+: architecture and applications
Camacho, C., Coulouris, G., Avagyan, V., Ma, N., Papadopoulos, J., Bealer, K., & Madden, T. L. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-421 · Cited by 22,074 · see citing works
David, F. N., & Tukey, J. W. (1977) · Biometrics · doi:10.2307/2529486 · Cited by 12,707 · see citing works
SignalP 4.0: discriminating signal peptides from transmembrane regions
Petersen, T. N., Brunak, S., von Heijne, G., & Nielsen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1701 · Cited by 8,847 · see citing works
UniProt: a hub for protein information
The UniProt Consortium (2015) · Nucleic Acids Research · doi:10.1093/nar/gku989 · Cited by 5,106 · see citing works
Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697 · see citing works
WoLF PSORT: protein localization predictor
Horton, P., Park, K., Obayashi, T., Fujita, N., Harada, H., Adams-Collier, C. J., & Nakai, K. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm259 · Cited by 4,154 · 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
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 3,967 · 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
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · 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
Semi-supervised learning for peptide identification from shotgun proteomics datasets
Käll, L., Canterbury, J. D., Weston, J., Noble, W. S., & MacCoss, M. J. (2007) · Nature Methods · doi:10.1038/nmeth1113 · Cited by 2,424 · see citing works
Self-citationWallace, D. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3365 · Cited by 2,404 · see citing works
Autophagosome formation: core machinery and adaptations
Xie, Z., & Klionsky, D. J. (2007) · Nature Cell Biology · doi:10.1038/ncb1007-1102 · Cited by 2,165 · see citing works
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994 · see citing works
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987 · see citing works
Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985 · 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
Osborn, J. F., & Tukey, J. (1978) · Journal of the Royal Statistical Society Series A (General) · doi:10.2307/2344492 · Cited by 1,782 · see citing works
Computational method to predict mitochondrially imported proteins and their targeting sequences.
Claros, M. G., & Vincens, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00779.x · Cited by 1,736 · 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
Selective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558 · see citing works
Using FlyAtlas to identify better Drosophila melanogaster models of human disease
Chintapalli, V. R., Wang, J., & Dow, J. A. T. (2007) · Nature Genetics · doi:10.1038/ng2049 · Cited by 1,479 · 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
Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342 · see citing works
MitoCarta2.0: an updated inventory of mammalian mitochondrial proteins
Calvo, S. E., Clauser, K. R., & Mootha, V. K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1003 · Cited by 1,251 · 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
Self-citationDiscovery of Atg5/Atg7-independent alternative macroautophagy
Nishida, Y., Arakawa, S., Fujitani, K., Yamaguchi, H., Mizuta, T., Kanaseki, T., Komatsu, M., Otsu, K., Tsujimoto, Y., & Shimizu, S. (2009) · Nature · doi:10.1038/nature08455 · Cited by 1,103 · see citing works
The role of mitochondria in aging
Bratic, A., & Larsson, N.-G. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64125 · Cited by 1,087 · see citing works
Choi, M., Chang, C.-Y., Clough, T., Broudy, D., Killeen, T., MacLean, B., & Olga Vitek, A. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu305 · Cited by 1,041 · see citing works
Predotar: A tool for rapidly screening proteomes for N‐terminal targeting sequences
Small, I., Peeters, N., Legeai, F., & Lurin, C. (2004) · Proteomics · doi:10.1002/pmic.200300776 · Cited by 913 · see citing works
Wagner, S., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., & Choudhary, C. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013284 · Cited by 889 · see citing works
CYTOPLASMIC COMPONENTS IN HEPATIC CELL LYSOSOMES
Ashford, T. P., & Porter, K. R. (1962) · The Journal of Cell Biology · doi:10.1083/jcb.12.1.198 · Cited by 849 · see citing works
An integrative approach to ortholog prediction for disease-focused and other functional studies
Hu, Y., Flockhart, I., Vinayagam, A., Bergwitz, C., Berger, B., Perrimon, N., & Mohr, S. E. (2011) · BMC Bioinformatics · doi:10.1186/1471-2105-12-357 · Cited by 801 · see citing works
A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes
Soubannier, V., McLelland, G., Zunino, R., Braschi, E., Rippstein, P. U., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 755 · see citing works
McLelland, G., Soubannier, V., Chen, C. X., McBride, H. M., & Fon, E. A. (2014) · The EMBO Journal · doi:10.1002/embj.201385902 · Cited by 743 · see citing works
Surface and inside volumes in globular proteins
Janin, J. (1979) · Nature · doi:10.1038/277491a0 · Cited by 714 · see citing works
Gene: a gene-centered information resource at NCBI
Brown, G., Hem, V., Katz, K., Ovetsky, M., Wallin, C., Ermolaeva, O. D., Tolstoy, I., Tatusova, T. A., Pruitt, K. D., Maglott, D. R., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1055 · Cited by 706 · see citing works
Sun, N., Yun, J., Liu, J., Malide, D. A., Liu, C., Rovira, I. I., Holmström, K. M., Fergusson, M. M., Yoo, Y. H., Combs, C. A., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.009 · Cited by 696 · see citing works
Nitric oxide‐induced mitochondrial fission is regulated by dynamin‐related GTPases in neurons
Barsoum, M. J., Yuan, H., Gerencser, A. A., Liot, G., Kushnareva, Y., Gräber, S., Kovács, I., Lee, W. D., Waggoner, J., Cui, J., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601253 · Cited by 658 · see citing works
Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612 · see citing works
mito-QC illuminates mitophagy and mitochondrial architecture in vivo
McWilliams, T. G., Prescott, A. R., Allen, G. F. G., Tamjar, J., Munson, M. J., Thomson, C., Muqit, M. M. K., & Ganley, I. G. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603039 · Cited by 541 · see citing works
The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 501 · 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
The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo
Vincow, E. S., Merrihew, G., Thomas, R. E., Shulman, N. J., Beyer, R. P., MacCoss, M. J., & Pallanck, L. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221132110 · Cited by 478 · see citing works
Juhász, G., Érdi, B., Sass, M., & Neufeld, T. P. (2007) · Genes & Development · doi:10.1101/gad.1600707 · Cited by 396 · see citing works
Proteomic Parsimony through Bipartite Graph Analysis Improves Accuracy and Transparency
Zhang, B., Chambers, M., & Tabb, D. L. (2007) · Journal of Proteome Research · doi:10.1021/pr070230d · Cited by 374 · see citing works
NucPred—Predicting nuclear localization of proteins
Brameier, M., Krings, A., & MacCallum, R. M. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm066 · Cited by 359 · see citing works
Analysis of proteome dynamics in the mouse brain
Price, J. C., Guan, S., Burlingame, A., Prusiner, S. B., & Ghaemmaghami, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006551107 · Cited by 357 · see citing works
Dai, D., Karunadharma, P. P., Chiao, Y. A., Basisty, N., Crispin, D. A., Hsieh, E. J., Chen, T., Gu, H., Djukovic, D., Raftery, D., et al. (2014) · Aging Cell · doi:10.1111/acel.12203 · Cited by 328 · see citing works
FlyBase: establishing a Gene Group resource for Drosophila melanogaster
Attrill, H. L., Falls, K. M., Goodman, J. L., Millburn, G., Antonazzo, G., Rey, A. J., & Marygold, S. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1046 · Cited by 322 · see citing works
Mitochondrial autophagy: Origins, significance, and role of BNIP3 and NIX
Ney, P. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.02.022 · Cited by 319 · 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
Ducret, A., van Oostveen, I., Eng, J. K., Yates, J. R., & Aebersold, R. H. (1998) · Protein Science · doi:10.1002/pro.5560070320 · Cited by 310 · see citing works
Requirement for the Yeast Gene LON in Intramitochondrial Proteolysis and Maintenance of Respiration
Suzuki, C. K., Suda, K., Wang, N., & Schatz, G. (1994) · Science · doi:10.1126/science.8146662 · Cited by 272 · see citing works
Fanconi Anemia Proteins Function in Mitophagy and Immunity
Sumpter, R., Sirasanagandla, S., Fernández, Á. F., Wei, Y., Dong, X., Franco, L., Zou, Z., Marchal, C., Lee, M. Y., Clapp, D. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.04.006 · Cited by 250 · see citing works
PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy
Kawajiri, S., Saiki, S., Sato, S., Sato, F., Hatano, T., Eguchi, H., & Hattori, N. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.016 · Cited by 246 · see citing works
Kuznetsov, A. V., & Margreiter, R. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10041911 · Cited by 242 · see citing works
Turnover of rat-liver mitochondria
Fletcher, M. J., & Sanadi, D. R. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90177-9 · Cited by 238 · see citing works
PINK1-induced mitophagy promotes neuroprotection in Huntington’s disease
Khalil, B., Fissi, N. E., Aouane, A., Cabirol-Pol, M.-J., Rival, T., & Liévens, J.-C. (2015) · Cell Death and Disease · doi:10.1038/cddis.2014.581 · Cited by 228 · see citing works
Tolkovsky, A. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.03.002 · Cited by 226 · see citing works
A Rab5 endosomal pathway mediates Parkin-dependent mitochondrial clearance
Hammerling, B. C., Najor, R. H., Cortez, M. Q., Shires, S. E., Leon, L. J., Gonzalez, E. R., Boassa, D., Phan, S., Thor, A., Jimenez, R. E., et al. (2017) · Nature Communications · doi:10.1038/ncomms14050 · Cited by 216 · see citing works
Prediction of Peroxisomal Targeting Signal 1 Containing Proteins from Amino Acid Sequence
Neuberger, G., Maurer‐Stroh, S., Eisenhaber, B., Hartig, A., & Eisenhaber, F. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00319-x · Cited by 213 · see citing works
Mitochondrial glutathione: Features, regulation and role in disease
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.018 · Cited by 205 · see citing works
Hämäläinen, R. H., Manninen, T., Koivumäki, H., Kislin, M., Otonkoski, T., & Suomalainen, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311660110 · Cited by 201 · see citing works
FlyAtlas: database of gene expression in the tissues of Drosophila melanogaster
Robinson, S. W., Herzyk, P., Dow, J., & Leader, D. (2012) · Nucleic Acids Res. · doi:10.1093/nar/gks1141 · Cited by 179 · see citing works
Metabolic Labeling Reveals Proteome Dynamics of Mouse Mitochondria
Kim, T., Wang, D., Kim, A. K., Lau, E., Lin, A. J., Liem, D. A., Zhang, J., Zong, C., Lam, M. P. Y., & Ping, P. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.021162 · Cited by 175 · see citing works
Motif Refinement of the Peroxisomal Targeting Signal 1 and Evaluation of Taxon-specific Differences
Neuberger, G., Maurer‐Stroh, S., Eisenhaber, B., Hartig, A., & Eisenhaber, F. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00318-8 · Cited by 169 · see citing works
Autophagosomal Content Profiling Reveals an LC3C-Dependent Piecemeal Mitophagy Pathway
Guerroué, F. L., Eck, F., Jung, J., Starzetz, T., Mittelbronn, M. G. A., Kaulich, M., & Behrends, C. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.029 · Cited by 150 · see citing works
Selective sorting and destruction of mitochondrial membrane proteins in aged yeast
Hughes, A. L., Hughes, C. E., Henderson, K. A., Yazvenko, N., & Gottschling, D. E. (2016) · eLife · doi:10.7554/elife.13943 · Cited by 149 · see citing works
Hsp90 Inhibition Decreases Mitochondrial Protein Turnover
Margineantu, D. H., Emerson, C. B., Diaz, D., & Hockenbery, D. M. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001066 · Cited by 147 · see citing works
Ferreira, R. M., Vitorino, R. M. P., Alves, R. M. P., Appell, H. J., Powers, S. K., Duarte, J. A., & Amado, F. M. L. (2010) · PROTEOMICS · doi:10.1002/pmic.201000173 · Cited by 145 · see citing works
Bit-by-bit autophagic removal of parkin-labelled mitochondria
Yang, J., & Yang, W. Y. (2013) · Nature Communications · doi:10.1038/ncomms3428 · Cited by 140 · 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
Erratum: Livermore Faces Forces of Change
Anderson, C. (1994) · Science · doi:10.1126/science.8178144 · Cited by 125 · see citing works
Comparison of Database Search Strategies for High Precursor Mass Accuracy MS/MS Data
Hsieh, E. J., Hoopmann, M. R., MacLean, B., & MacCoss, M. J. (2009) · Journal of Proteome Research · doi:10.1021/pr900816a · Cited by 123 · see citing works
The Metabolism of Mitochondrial Proteins
Swick, R. W., Rexroth, A. K., & Stange, J. L. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34180-8 · Cited by 119 · see citing works
Abeliovich, H., Zarei, M., Rigbolt, K. T. G., Youle, R. J., & Dengjel, J. (2013) · Nature Communications · doi:10.1038/ncomms3789 · Cited by 119 · see citing works
What can mitochondrial heterogeneity tell us about mitochondrial dynamics and autophagy?
Wikström, J. D., Twig, G., & Shirihai, O. S. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.06.006 · Cited by 113 · see citing works
Oxidative Stress, Mitochondrial Dysfunction and the Mitochondria Theory of Aging
Kong, Y., Trabucco, S. E., & Zhang, H. (2014) · Interdisciplinary topics in gerontology and geriatrics · doi:10.1159/000358901 · Cited by 112 · see citing works
CONTROL OF MITOCHONDRIAL TURNOVER UNDER THE INFLUENCE OF THYROID HORMONE
Gross, N. J. (1971) · The Journal of Cell Biology · doi:10.1083/jcb.48.1.29 · Cited by 107 · see citing works
Turnover of Protein and Ribonucleic Acid in Synaptic Subcellular Fractions from Rat Brain
von Hungen, K., Mahler, H. R., & Moore, W. J. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93560-x · Cited by 101 · see citing works
McCune, H. J., Danielson, L. S., Alvino, G. M., Collingwood, D., Delrow, J. J., Fangman, W. L., Brewer, B. J., & Raghuraman, M. K. (2008) · Genetics · doi:10.1534/genetics.108.094359 · Cited by 100 · see citing works
Characterization of Peptides Released from Mitochondria
Augustin, S., Nolden, M., Müller, S., Hardt, O., Arnold, I., & Langer, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410609200 · Cited by 99 · see citing works
Importing ArrayExpress datasets into R/Bioconductor
Kauffmann, A., Rayner, T. F., Parkinson, H., Kapushesky, M., Lukk, M., Brāzma, A., & Huber, W. K. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp354 · Cited by 98 · see citing works
Karunadharma, P. P., Basisty, N., Dai, D., Chiao, Y. A., Quarles, E. K., Hsieh, E. J., Crispin, D. A., Bielas, J. H., Ericson, N. G., Beyer, R. P., et al. (2015) · Aging Cell · doi:10.1111/acel.12317 · Cited by 79 · see citing works
Mechanisms of In Vivo Ribosome Maintenance Change in Response to Nutrient Signals
Mathis, A. D., Naylor, B. C., Carson, R. H., Evans, E., Harwell, J., Knecht, J., Hexem, E., Peelor, F. F., Miller, B. F., Hamilton, K. L., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.063255 · Cited by 79 · see citing works
Degradation Rate of Mitochondrial Proteins in Arabidopsis thaliana Cells
Nelson, C. J., Li, L., Jacoby, R. P., & Millar, A. H. (2013) · Journal of Proteome Research · doi:10.1021/pr400304r · Cited by 76 · see citing works
Age modifies respiratory complex I and protein homeostasis in a muscle type‐specific manner
Kruse, S. E., Karunadharma, P. P., Basisty, N., Johnson, R. S., Beyer, R. P., MacCoss, M. J., Rabinovitch, P. S., & Marcinek, D. J. (2015) · Aging Cell · doi:10.1111/acel.12412 · Cited by 73 · see citing works
Outer Mitochondrial Membrane Protein Degradation by the Proteasome
Neutzner, A., Youle, R. J., & Karbowski, M. (2007) · Novartis Foundation symposium · doi:10.1002/9780470725207.ch2 · Cited by 72 · see citing works
Global Analysis of Cellular Protein Flux Quantifies the Selectivity of Basal Autophagy
Zhang, T., Shen, S., Qu, J., & Ghaemmaghami, S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.040 · Cited by 70 · see citing works
Karunadharma, P. P., Basisty, N., Chiao, Y. A., Dai, D., Drake, R., Levy, N., Koh, W. J. H., Emond, M. J., Kruse, S. E., Marcinek, D. J., et al. (2015) · The FASEB Journal · doi:10.1096/fj.15-272666 · Cited by 69 · see citing works
Collins, M. L., Eng, S., Hoh, R., & Hellerstein, M. K. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00691.2002 · Cited by 68 · see citing works
Using FlyBase, a Database of Drosophila Genes and Genomes
Marygold, S. J., Crosby, M. A., & Goodman, J. L. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6371-3_1 · Cited by 68 · see citing works
Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane
Shi, H., Rampello, A. J., & Glynn, S. E. (2016) · Nature Communications · doi:10.1038/ncomms13301 · Cited by 62 · see citing works
Érdi, B., Nagy, P., Zvara, Á., Varga, Á., Pircs, K., Ménesi, D., Puskás, L. G., & Juhász, G. (2012) · Autophagy · doi:10.4161/auto.20069 · Cited by 60 · see citing works
Alternative Macroautophagic Pathways
Juenemann, K., & Reits, E. A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/189794 · Cited by 58 · see citing works
Hsieh, E. J., Shulman, N., Dai, D., Vincow, E. S., Karunadharma, P. P., Pallanck, L. J., Rabinovitch, P. S., & MacCoss, M. J. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.017699 · Cited by 56 · see citing works
Choe, S. C., Hamacher‐Brady, A., & Brady, N. R. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0115-9 · Cited by 54 · see citing works
Sardiello, M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg123 · Cited by 53 · see citing works
Mitochondrial proteases and cancer
Bulteau, A., & Bayot, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.12.011 · Cited by 52 · see citing works
Mitochondrial quality control in neurodegenerative diseases.
Dupuis, L. (2014) · Biochimie · doi:10.1016/j.biochi.2013.07.033 · Cited by 51 · see citing works
Clarke, K. J., Adams, A. E., Manzke, L. H., Pearson, T. W., Borchers, C. H., & Porter, R. K. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.03.035 · Cited by 46 · see citing works
STUDIES OF TURNOVER IN MAMMALIAN SUBCELLULAR PARTICLES: BRAIN NUCLEI, MITOCHONDRIA AND MICROSOMES*
Khan, A. A., & Wilson, J. E. (1965) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1965.tb11942.x · Cited by 35 · see citing works
HETEROGENEITY AND DIFFERENTIAL FRAGILITY OF RAT LIVER MITOCHONDRIA
LUSENA, C. V., & Depocas, F. (1966) · Canadian Journal of Biochemistry · doi:10.1139/o66-060 · Cited by 34 · see citing works
Is mitochondrial DNA turnover slower than commonly assumed?
Poovathingal, S. K., Gruber, J., Lakshmanan, L. N., Halliwell, B. B., & Gunawan, R. (2012) · Biogerontology · doi:10.1007/s10522-012-9390-7 · Cited by 33 · see citing works
Rampello, A. J., & Glynn, S. E. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.02.009 · Cited by 30 · see citing works
Separate-channel analysis of two-channel microarrays: recovering inter-spot information
Smyth, G. K., & Altman, N. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-165 · Cited by 29 · see citing works
How the proteasome is degraded
Hoeller, D., & Đikić, I. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616535113 · Cited by 22 · see citing works
“High-Throughput Characterization of Region-Specific Mitochondrial Function and Morphology”
Daniele, J. R., Esping, D. J., Garcia, G., Parsons, L. S., Arriaga, E. A., & Dillin, A. G. (2017) · Scientific Reports · doi:10.1038/s41598-017-05152-z · Cited by 19 · see citing works
Mitophagy as a stress response in mammalian cells and in respiring S. cerevisiae
Abeliovich, H., & Dengjel, J. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150278 · Cited by 11 · see citing works
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- Tolkovsky AM. Mitophagy. Biochim Biophys Acta. 2009 Sep;1793 (9):1508-1515.
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Sorted by citations
The role of PINK1–Parkin in mitochondrial quality control
Narendra, D. P., & Youle, R. J. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01513-9 · Cited by 580 · 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
Outstanding Questions in Mitophagy: What We Do and Do Not Know
Montava‐Garriga, L., & Ganley, I. G. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.032 · Cited by 209 · 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
Mitochondria—Striking a balance between host and endosymbiont
Youle, R. J. (2019) · Science · doi:10.1126/science.aaw9855 · Cited by 192 · see citing works
Goldsmith, J., Ordureau, A., Harper, J. W., & Holzbaur, E. L. F. (2022) · Neuron · doi:10.1016/j.neuron.2021.12.029 · Cited by 105 · see citing works
BNIP3 promotes HIF‐1α‐driven melanoma growth by curbing intracellular iron homeostasis
Vara‐Pérez, M., Rossi, M., den Haute, C. V., Maes, H., Sassano, M. L., Venkataramani, V., Michalke, B., Romano, E., Rillaerts, K., Garg, A. D., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106214 · Cited by 89 · see citing works
Mt-Keima detects PINK1-PRKN mitophagy in vivo with greater sensitivity than mito-QC
Liu, Y., Sliter, D. A., Shammas, M. K., Huang, X., Wang, C., Calvelli, H. R., Maric, D., & Narendra, D. P. (2021) · Autophagy · doi:10.1080/15548627.2021.1896924 · Cited by 81 · see citing works
Structural Mechanisms of Mitochondrial Quality Control Mediated by PINK1 and Parkin
Trempe, J., & Gehring, K. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168090 · Cited by 58 · see citing works
From mitochondria to sarcopenia: role of 17β-estradiol and testosterone
Tian, X., Lou, S., & Shi, R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1156583 · Cited by 54 · see citing works
“A recent proteomics-based study of Drosophila fibroblasts found that approximately 70% of mitochondrial protein turnover occurs through non-autophagic degradation processes such as mitoproteases and UPS; Autophagy accounts for about 30% of mitochondrial protein turnover (54).”
BackgroundLi, H., Doric, Z., Berthet, A., Jorgens, D. M., Nguyen, M. K., Hsieh, I., Margulis, J., Fang, R., Debnath, J., Sesaki, H., et al. (2021) · Science Advances · doi:10.1126/sciadv.abf6580 · Cited by 42 · see citing works
SnRK1 and TOR: central regulators of autophagy in plant energy stress responses
Feng, L., Li, X., Zheng, X., Zheng, Z., Liu, Q.-R., Liu, C., Zhu, Q.-L., Shen, W., Yang, C., Li, H., et al. (2025) · aBIOTECH · doi:10.1007/s42994-025-00218-3 · Cited by 35 · see citing works
Phosphorylation of mitochondrial matrix proteins regulates their selective mitophagic degradation
Kolitsida, P., Zhou, J., Rackiewicz, M., Nolić, V., Dengjel, J., & Abeliovich, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901759116 · Cited by 28 · see citing works
Molecular mechanisms of selective autophagy in Drosophila
Gohel, R., Kournoutis, A., Petridi, S., & Nezis, I. P. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2019.08.003 · Cited by 27 · see citing works
Terriente-Félix, A., Wilson, E. L., & Whitworth, A. J. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008844 · Cited by 27 · see citing works
Roberts, R. F., Bayne, A. N., Goiran, T., Lévesque, D., Boisvert, F., Trempe, J., & Fon, E. A. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00506 · Cited by 26 · see citing works
TSG101 negatively regulates mitochondrial biogenesis in axons
Lin, T.-H., Bis‐Brewer, D. M., Sheehan, A. E., Townsend, L., Maddison, D. C., Zuchner, S. L., Smith, G. A., & Freeman, M. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2018770118 · Cited by 26 · see citing works
Mitochondrial dynamics and quality control regulate proteostasis in neuronal ischemia-reperfusion
Fogo, G. M., Raghunayakula, S., Emaus, K. J., Torres, F. J. T., Shangguan, G., Wider, J. M., Hüttemann, M., & Sanderson, T. H. (2025) · Autophagy · doi:10.1080/15548627.2025.2472586 · Cited by 26 · see citing works
Groennebaek, T., Nielsen, J., Jespersen, N. R., Bøtker, H. E., de Paoli, F. V., Miller, B. F., & Vissing, K. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00101.2020 · Cited by 25 · see citing works
Insolera, R., Lőrincz, P., Wishnie, A. J., Juhász, G., & Collins, C. A. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009731 · Cited by 25 · see citing works
Pareek, G., & Pallanck, L. J. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009118 · Cited by 22 · see citing works
Li, L., Lee, C. P., Ding, X., Yu, Q., Yapa, A. W., Broda, M., Otegui, M. S., & Millar, A. H. (2022) · The Plant Cell · doi:10.1093/plcell/koac185 · Cited by 19 · see citing works
Managing risky assets – mitophagy in vivo
Narendra, D. P. (2021) · Journal of Cell Science · doi:10.1242/jcs.240465 · Cited by 16 · see citing works
The memory- and cognition-facilitating effects of spermidine in aging and aging-related disorders
Zou, M., Li, D., & Yang, Y. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102787 · Cited by 17 · see citing works
Slowed Protein Turnover in Aging Drosophila Reflects a Shift in Cellular Priorities
Vincow, E. S., Thomas, R. E., Merrihew, G. E., MacCoss, M. J., & Pallanck, L. J. (2021) · The Journals of Gerontology Series A · doi:10.1093/gerona/glab015 · Cited by 16 · see citing works
AAA+ proteases: the first line of defense against mitochondrial damage
Pareek, G. (2022) · PeerJ · doi:10.7717/peerj.14350 · Cited by 14 · see citing works
Gospodaryov, D. V. (2024) · Biochimica et Biophysica Acta - Bioenergetics · doi:10.1016/j.bbabio.2024.149529 · Cited by 13 · see citing works
Phillips, M., Arnold, K. R., Vue, Z., Beasley, H. K., Lopez, E. G., Marshall, A. G., Morton, D. J., McReynolds, M. R., Barter, T. T., & Hinton, A. O., Jr. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031067 · Cited by 13 · see citing works
The pyruvate dehydrogenase complex regulates mitophagic trafficking and protein phosphorylation
Kolitsida, P., Nolić, V., Zhou, J., Stumpe, M., Niemi, N. M., Dengjel, J., & Abeliovich, H. (2023) · Life Science Alliance · doi:10.26508/lsa.202302149 · Cited by 11 · see citing works
Physiological functions of mitophagy
Stanojlović, M., Bishnu, A., Singh, F., & Ganley, I. G. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100612 · Cited by 10 · see citing works
Goldsmith, J., Ordureau, A., Boecker, C. A., Arany, M., Harper, J. W., & Holzbaur, E. L. F. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.03.510717 · Cited by 10 · see citing works
Sen, A., & Cox, R. T. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1004099 · Cited by 7 · see citing works
Detection of mitophagy in mammalian cells, mice, and yeast
Calvelli, H. R., Krigman, J., Onishi, M., Narendra, D. P., Sun, N., & Okamoto, K. (2019) · Methods in cell biology · doi:10.1016/bs.mcb.2019.10.006 · Cited by 6 · see citing works
Comment on “mt-Keima detects PINK1-PRKN mitophagy in vivo with greater sensitivity than mito-QC”
Liu, Y., Sliter, D. A., Shammas, M. K., Huang, X., Wang, C., Calvelli, H. R., Maric, D., & Narendra, D. P. (2021) · Autophagy · doi:10.1080/15548627.2021.1909999 · Cited by 6 · see citing works
In vivo assay and modelling of protein and mitochondrial turnover during aging
Bell, H. S., & Tower, J. (2021) · Fly · doi:10.1080/19336934.2021.1911286 · Cited by 6 · see citing works
Insights into PINK1/Parkin function and dysfunction from Drosophila models
Park, S., Kozhushko, N., Wight, T. H., & Whitworth, A. J. (2025) · Biochemical Journal · doi:10.1042/bcj20253459 · Cited by 4 · see citing works
Analysis of Mitochondrial Dynamics in AdultDrosophilaAxonsPreprint
Maddison, D. C., Mattedi, F., Vagnoni, A., & Smith, G. A. (2022) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top107819 · Cited by 3 · see citing works
Laine-Menéndez, S., la Torre, M. F.-D., Fiuza‐Luces, C., Delmiro, A., Arenas, J., Martín, M. A., Boya, P., Lucía, A., & Morán, M. (2022) · Antioxidants · doi:10.3390/antiox11030510 · Cited by 2 · see citing works
Acheampong, H. O., Rozich, E., Haupt, Z., Tokarz, C., Khan, M., Ghosn, Z. A., & Insolera, R. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e25-05-0235 · Cited by 1 · see citing works
Lando, A. P., Maritano, P. C., Barbieri, G., Daloso, D. M., Martínez-Noël, G. M. A., & Rodriguez, M. S. (2026) · Plant Science · doi:10.1016/j.plantsci.2026.113129 · Cited by 1 · see citing works
Wang, T. S., Coppens, I., Brady, N. R., & Hamacher‐Brady, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.23.538008 · Cited by 1 · see citing works
Exercise and Mitochondrial Function: Importance and Inference- A Mini Review
Vaishali, K., Kumar, N., Rao, V., Kovela, R. K., & Sinha, M. K. (2021) · Current Molecular Medicine · doi:10.2174/1566524021666211129110542
Kolitsida, P., Nolić, V., Zhou, J., Stumpe, M., Niemi, N. M., Dengjel, J., & Abeliovich, H. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.16.484611
Saxena, R. R., & Saxena, R. (2023) · IJRDO - Journal of Biological Science · doi:10.53555/bs.v1i1.5937
PINK1-Parkin quality control mitophagy pathway in Parkinson’s disease
Thayer, J. A., & Narendra, D. P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00013-2
Illuminating the Role of Asymmetric Mitochondrial Fission on Beta-Cell HealthPreprint
Henning, P., Schultz, J., Baltrusch, S., & Uhrmacher, A. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.25.690461
Rab12 is a regulator of mitophagy and mitochondrial homeostasisPreprint
Richbourg, T., George, A., Bitar, A., Ryde, I. T., Farrell, C., Malankhanova, T. B., Liu, J., Buck, S. A., Barraza, I., Kim, S. Y. A., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.29.715103
Henning, P., Schultz, J., Baltrusch, S., & Uhrmacher, A. M. (2026) · npj Systems Biology and Applications · doi:10.1038/s41540-026-00732-0
Acheampong, H. O., Rozich, E., & Insolera, R. (2026) · Research Square · doi:10.21203/rs.3.rs-9407058/v1
Burks, E., Copes, J., Nguyen, K., Tawil-Brown, A., & Yan, S. (2026) · Autophagy Reports · doi:10.1080/27694127.2026.2698350 · Cited by 1 · see citing works
Otele, I. M., Patel, T., Arshad, M. S., Ahmad, Z., Banu, H., & Singh, N. (2026) · Journal of Cluster Science · doi:10.1007/s10876-026-03111-1
- Authors
- Vincow, E. S., Thomas, R. E., Merrihew, G. E., Shulman, N. J., Bammler, T. K., MacDonald, J. W., MacCoss, M. J., & Pallanck, L. J.
- Affiliations
- University of Washington (US)
- Corresponding author
- Pallanck, Leo J.
- ORCID
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2019-03-21
- Volume
- 15
- Issue
- 9
- Pages
- 1592-1605
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC6693455
- OpenAlex
- W2921505376
- Cited by
- 54
- References
- 113
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 3 · 2023: 6 · 2022: 13 · 2021: 10 · 2020: 6 · 2019: 4
- FWCI
- 6.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1R01GM104990, 1RO1GM086394)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- mitochondrial protein turnover, selective autophagy, mitophagy, Parkin, PINK1, ATG7, ATG5, mitochondrial degradation, Drosophila melanogaster, human fibroblasts, proteomics, mitochondrial dysfunction, ubiquitination, YME1L, LC3B
- MeSH terms
- Autophagy-Related Protein 5, Autophagy-Related Protein 7, Animals, Drosophila melanogaster, Fibroblasts, Humans, Mitochondria, Models, Genetic, Organ Specificity, Proteome, Mitochondrial Proteins, Drosophila Proteins, Ubiquitin-Protein Ligases, Proteolysis, Mitophagy
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