Loss of Fis1 impairs proteostasis during skeletal muscle aging in Drosophila
Open accessAbstract
Increased levels of dysfunctional mitochondria within skeletal muscle are correlated with numerous age-related physiopathological conditions. Improving our understanding of the links between mitochondrial function and muscle proteostasis, and the role played by individual genes and regulatory networks, is essential to develop treatments for these conditions. One potential player is the mitochondrial outer membrane protein Fis1, a crucial fission factor heavily involved in mitochondrial dynamics in yeast but with an unknown role in higher-order organisms. By using Drosophila melanogaster as a model, we explored the effect of Fis1 mutations generated by transposon Minos-mediated integration. Mutants exhibited a higher ratio of damaged mitochondria with age as well as elevated reactive oxygen species levels compared with controls. This caused an increase in oxidative stress, resulting in large accumulations of ubiquitinated proteins, accelerated muscle function decline, and mitochondrial myopathies in young mutant flies. Ectopic expression of Fis1 isoforms was sufficient to suppress this phenotype. Loss of Fis1 led to unbalanced mitochondrial proteostasis within fly muscle, decreasing both flight capabilities and lifespan. Fis1 thus clearly plays a role in fly mitochondrial dynamics. Further investigations into the detailed function of Fis1 are necessary for exploring how mitochondrial function correlates with muscle health during aging.
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?
Loss of FIS1 results in impaired mitochondrial function and proteostasis in muscle, decreasing both flight capabilities and lifespan in FIS1 mutant flies.
“Another recent study revealed that loss of FIS1 results in impaired mitochondrial function and proteostasis in muscle, decreasing both flight capabilities and lifespan in FIS1 mutant flies (89).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [89]
Mitochondrial fission is essential for skeletal muscle health.
“Taken altogether, the findings discussed above clearly indicate that mitochondrial fission is essential for skeletal muscle health.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [45]
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
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
Signals from chloroplasts converge to regulate nuclear gene expression.
Koussevitzky, S., Nott, A., Mockler, T. C., Hong, F., Sachetto‐Martins, G., Surpin, M. A., Lim, J. C.-S., Mittler, R., & Chory, J. (2007) · PubMed · doi:10.1126/science.1140516 · Cited by 5,076 · see citing works
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · 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
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · 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
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · cited 1× · see citing works
“…triphosphatases (GTPases) of the dynamin family (Chan, 2012; Kraus & Ryan, 2017; Ni et al., 2015; Pernas & Scorrano, 2016; Tilokani et al., 2018; Westermann, 2010), which are highly conserved in yeast, flies, and mammals (Hales & Fuller, 1997; Hoppins et al., 2007; Liesa et al., 2009; Zhao et…”
BackgroundFree Radical Lipid Peroxidation: Mechanisms and Analysis
Yin, H., Xu, L., & Porter, N. A. (2011) · Chemical Reviews · doi:10.1021/cr200084z · Cited by 1,952 · 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
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472 · see citing works
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110 · see citing works
Benedetti, A., Comporti, M., & Esterbauer, H. (1980) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(80)90209-x · Cited by 1,085 · see citing works
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953 · 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
Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 814 · see citing works
The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790 · see citing works
Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
Henchcliffe, C., & Beal, M. F. (2008) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0924 · Cited by 786 · see citing works
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778 · see citing works
Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737 · see citing works
Mozdy, A. D., McCaffery, J. M., & Shaw, J. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.367 · Cited by 725 · 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
Venken, K. J. T., Schulze, K. L., Haelterman, N. A. T., Pan, H., He, Y., Evans-Holm, M. E., Carlson, J. W., Levis, R. W., Spradling, A. C., Hoskins, R. A., et al. (2011) · Nature Methods · doi:10.1038/nmeth.1662 · Cited by 677 · see citing works
Keap1/Nrf2 Signaling Regulates Oxidative Stress Tolerance and Lifespan in Drosophila
Sykiotis, G. P., & Bohmann, D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.12.002 · Cited by 675 · see citing works
Protein misfolding in neurodegenerative diseases: Implications and strategies
Sweeney, P., Park, H., Baumann, M., Dunlop, J., Frydman, J., Kopito, R., McCampbell, A., Leblanc, G., Venkateswaran, A., Nurmi, A., et al. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0077-5 · Cited by 675 · see citing works
Guo, X., Winkler, C. A., Li, J., Guan, L., Tang, M., Liao, J., Deng, H., de Thé, G., Zeng, Y., & O’Brien, S. J. (2014) · BioMed Research International · doi:10.1155/2014/434072 · Cited by 667 · see citing works
Self-citationhFis1, a Novel Component of the Mammalian Mitochondrial Fission Machinery
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303758200 · Cited by 653 · see citing works
PINK1- and Parkin-mediated mitophagy at a glance
Jin, S. M., & Youle, R. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.093849 · Cited by 631 · see citing works
Developmentally Regulated Mitochondrial Fusion Mediated by a Conserved, Novel, Predicted GTPase
Hales, K. G., & Fuller, M. T. (1997) · Cell · doi:10.1016/s0092-8674(00)80319-0 · Cited by 611 · see citing works
Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, G. A., Vogel, H. S., & Lu, B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711845105 · Cited by 536 · see citing works
Regulation of brain mitochondrial H 2 O 2 production by membrane potential and NAD(P)H redox state
Starkov, A. A., & Fiskum, G. M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01908.x · Cited by 491 · see citing works
Mitofusins, from Mitochondria to Metabolism
Schrepfer, E., & Scorrano, L. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.022 · Cited by 490 · see citing works
Hauptmann, S., Scherping, I., Dröse, S., Brandt, U., Schulz, K. L., Jendrach, M., Leuner, K., Eckert, A., & Müller, W. E. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.12.005 · Cited by 469 · see citing works
The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway
Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010054 · Cited by 440 · see citing works
DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass
Favaro, G., Romanello, V., Varanita, T., Andrea Desbats, M., Morbidoni, V., Tezze, C., Albiero, M., Canato, M., Gherardi, G., De Stefani, D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10226-9 · Cited by 398 · see citing works
Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
Stojanovski, D., Koutsopoulos, O. S., Okamoto, K., & Ryan, M. T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01058 · Cited by 332 · see citing works
A Synthetic Maternal-Effect Selfish Genetic Element Drives Population Replacement in Drosophila
Chen, C., Huang, H., Ward, C. M., Su, J. T., Schaeffer, L., Guo, M., & Hay, B. A. (2007) · Science · doi:10.1126/science.1138595 · Cited by 319 · see citing works
Self-citationSingle Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging
Murgia, M., Toniolo, L., Nagaraj, N., Ciciliot, S., Vindigni, V., Schiaffino, S., Reggiani, C., & Mann, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.054 · Cited by 315 · see citing works
Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease
Reddy, P. H. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.042 · Cited by 264 · see citing works
Human Fis1 regulates mitochondrial dynamics through inhibition of the fusion machinery
Yu, R., Jin, S., Lendahl, U., Nistér, M., & Zhao, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899748 · Cited by 246 · see citing works
The constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244 · see citing works
High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy
Gomes, L. C., & Scorrano, L. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.05.442 · Cited by 239 · see citing works
Biology of Ageing and Role of Dietary Antioxidants
Peng, C., Wang, X., Chen, J., Jiao, R., Wang, L., Li, Y. M., Zuo, Y., Liu, Y., Lei, L., Ma, K. Y., et al. (2014) · BioMed Research International · doi:10.1155/2014/831841 · Cited by 226 · see citing works
Role of Oxidative Stress as Key Regulator of Muscle Wasting during Cachexia
Ábrigo, J., Elorza, Á. A., Riedel, C. A., Vilos, C., Simón, F., Cabrera, D., Estrada, L. D., & Cabello‐Verrugio, C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2063179 · Cited by 221 · see citing works
Causal roles of mitochondrial dynamics in longevity and healthy aging
Sharma, A., Smith, H. J., Yao, P., & Mair, W. B. (2019) · EMBO Reports · doi:10.15252/embr.201948395 · Cited by 214 · see citing works
Mutations in Fis1 disrupt orderly disposal of defective mitochondria
Shen, Q., Yamano, K., Head, B. P., Kawajiri, S., Cheung, J. T. M., Wang, C., Cho, J.-H., Hattori, N., Youle, R. J., & van der Bliek, A. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0525 · Cited by 209 · see citing works
Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model
Xie, H., Guan, J., Borrelli, L. A., Xu, J., Serrano-Pozo, A., & Bacskai, B. J. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1836-13.2013 · Cited by 185 · cited 1× · see citing works
“Several AD animal models and AD patient brains have exhibited evidence of reduced ATP concentration, diminished complex IV activity, and enhanced oxidative stress compared with controls (Hauptmann et al., 2009; Reddy, 2009; Xie et al., 2013).”
BackgroundSuzuki, M., Jeong, S.-Y., Karbowski, M., Youle, R. J., & Tjandra, N. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.064 · Cited by 161 · see citing works
Lo Verso, F., Carnio, S., Vainshtein, A., & Sandri, M. (2014) · Autophagy · doi:10.4161/auto.32154 · Cited by 146 · see citing works
Joshi, A. U., Saw, N. L., Shamloo, M., & Mochly‐Rosen, D. (2017) · Oncotarget · doi:10.18632/oncotarget.23640 · Cited by 146 · see citing works
STX17 dynamically regulated by Fis1 induces mitophagy via hierarchical macroautophagic mechanism
Xian, H., Yang, Q., Xiao, L., Shen, H., & Liou, Y. (2019) · Nature Communications · doi:10.1038/s41467-019-10096-1 · Cited by 135 · see citing works
Impaired proteostasis during skeletal muscle aging
Fernando, R., Drescher, C., Nowotny, K., Grune, T., & Castro, J. P. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.037 · Cited by 134 · see citing works
Wong-Riley, M., Antuono, P., Ho, K.-C., Egan, R., Hevner, R., Liebl, W., Huang, Z., Rachel, R., & Jones, J. L. (1997) · Vision Research · doi:10.1016/s0042-6989(96)00210-6 · Cited by 127 · see citing works
Regulation of mitochondrial dynamics: convergences and divergences between yeast and vertebrates
Zhao, J., Lendahl, U., & Nistér, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1066-6 · Cited by 99 · see citing works
Dulac, M., Leduc‐Gaudet, J., Reynaud, O., Ayoub, M., Guérin, A., Finkelchtein, M., Hussain, S. N., & Gouspillou, G. (2020) · The Journal of Physiology · doi:10.1113/jp279802 · Cited by 90 · cited 3× · see citing works
“In addition, the number of centrally nucleated myofibers has been used as a marker to reflect previous cycles of muscle degeneration and regeneration (Dulac et al., 2020; Favaro et al., 2019; Sakellariou et al., 2011).”
BackgroundMethodVainshtein, A., Grumati, P., Sandri, M., & Bonaldo, P. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1096-z · Cited by 88 · see citing works
Luceri, C., Bigagli, E., Femia, A. P., Caderni, G., Giovannelli, L., & Lodovici, M. (2018) · Toxicology Reports · doi:10.1016/j.toxrep.2017.12.017 · Cited by 79 · see citing works
Sakellariou, G. K., Pye, D., Vasilaki, A., Zibrik, L., Palomero, J., Kabayo, T., McArdle, F., Remmen, H. V., Richardson, A. G., Tidball, J. G., et al. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00709.x · Cited by 75 · see citing works
Wang, S., Song, J., Tan, M., Albers, K. M., & Jia, J. (2012) · European Journal of Neurology · doi:10.1111/j.1468-1331.2012.03670.x · Cited by 64 · see citing works
Ubiquitin sets the timer: impacts on aging and longevity
Kevei, É., & Hoppe, T. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2806 · Cited by 61 · see citing works
Mitochondrial fission facilitates mitophagy inSaccharomyces cerevisiae
Mao, K., & Klionsky, D. J. (2013) · Autophagy · doi:10.4161/auto.25804 · Cited by 60 · see citing works
MCM2-regulated functional networks in lung cancer by multi-dimensional proteomic approach
Cheung, C. H. Y., Hsu, C., Chen, K.-P., Chong, S.-T., Wu, C.-H., Huang, H., & Juan, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-13440-x · Cited by 44 · see citing works
Self-citationFis1 deficiencies differentially affect mitochondrial quality in skeletal muscle
Zhang, Z., Sliter, D. A., Bleck, C. K. E., & Ding, S. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.09.005 · Cited by 41 · see citing works
Reichart, G., Mayer, J., Zehm, C., Kirschstein, T., Tokay, T., Lange, F., Baltrusch, S., Tiedge, M., Fuellen, G., Ibrahim, S. M., et al. (2018) · Acta Physiologica · doi:10.1111/apha.13214 · Cited by 39 · see citing works
Inhibition of the deubiquitinase USP8 corrects a Drosophila PINK1 model of mitochondria dysfunction
von Stockum, S., Sánchez-Martínez, Á., Corrà, S., Chakraborty, J., Marchesan, E., Locatello, L., Da‐Ré, C., Cusumano, P., Caicci, F., Ferrari, V., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900392 · Cited by 31 · see citing works
Self-citationChai, N., Haney, M. S., Couthouis, J., Morgens, D. W., Benjamin, A., Wu, K., Ousey, J., Fang, S., Finer, S., Bassik, M. C., et al. (2020) · Brain Research · doi:10.1016/j.brainres.2019.146601 · Cited by 26 · see citing works
A Colorimetric Assay of Citrate Synthase Activity in Drosophila Melanogaster
Wei, P. Y., Liu, Q., Xue, W., & Wang, J. (2020) · Journal of Visualized Experiments · doi:10.3791/59454 · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
“Another recent study showed that loss of Fis1 leads to mitochondrial dysfunction, proteostasis impairment, muscle degeneration, and reduced lifespan in Fis1 mutant flies [45].”
BackgroundLei, Y., Gan, M., Qiu, Y., Chen, Q., Wang, X., Liao, T., Zhao, M., Chen, L., Zhang, S., Zhao, Y., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00572-y · Cited by 102 · see citing works
Mitophagy in aging and longevity
Guo, J., & Chiang, W. (2021) · IUBMB Life · doi:10.1002/iub.2585 · 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
“Another recent study revealed that loss of FIS1 results in impaired mitochondrial function and proteostasis in muscle, decreasing both flight capabilities and lifespan in FIS1 mutant flies (89).”
BackgroundImplications of mitochondrial fusion and fission in skeletal muscle mass and health
Romanello, V., & Sandri, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.011 · Cited by 44 · 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
Wu, Z., Li, Y.-C., Zheng, Y., Zhou, M., Li, H. Z., Wu, S.-X., Zhao, X., Yang, Y., & Du, L. (2024) · Food & Function · doi:10.1039/d4fo04341c · Cited by 20 · see citing works
Cellular senescence: from homeostasis to pathological implications and therapeutic strategies
Li, C., Yuan, Y., Jia, Y., Zhou, Q., Wang, Q., & Jiang, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1534263 · Cited by 20 · see citing works
Xiong, H., Qiu, H., Wang, C., Qiu, Y., Tan, S., Chen, K., Zhao, F., & Song, J. (2024) · Materials Today Bio · doi:10.1016/j.mtbio.2024.101175 · Cited by 18 · see citing works
Identification of evolutionarily conserved regulators of muscle mitochondrial network organization
Katti, P., Ajayi, P. T., Aponte, A. M., Bleck, C. K. E., & Glancy, B. C. (2022) · Nature Communications · doi:10.1038/s41467-022-34445-9 · Cited by 16 · see citing works
Mitophagy: A Bridge Linking HMGB1 and Parkinson’s Disease Using Adult Zebrafish as a Model Organism
Razali, K., Nasir, M. H. M., Kumar, J., & Mohamed, W. M. Y. (2023) · Brain Sciences · doi:10.3390/brainsci13071076 · Cited by 15 · see citing works
Advances in Human Mitochondria-Based Therapies
Zhong, G., Venkatesan, J. K., Madry, H., & Cucchiarini, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010608 · Cited by 13 · see citing works
Wen, D., Gao, Y., Wang, J., Wang, S., Zhong, Q., & Hou, W.-Q. (2023) · Genes & Nutrition · doi:10.1186/s12263-023-00725-2 · Cited by 12 · see citing works
Chen, Q., Huang, W., Çapanoğlu, E., Amrouche, A. T., & Lu, B. (2023) · Food Frontiers · doi:10.1002/fft2.261 · Cited by 12 · see citing works
Pan, Y., Liu, P., Li, S., Li, B., Li, Y., & Ma, L. (2023) · European journal of medical research · doi:10.1186/s40001-023-01021-w · Cited by 12 · see citing works
Wu, S.-C., Chen, Y.-J., Su, S.-H., Fang, P.-H., Liu, R.-W., Tsai, H.-Y., Chang, Y.-J., Li, H.-H., Li, J., & Chen, C. (2025) · Communications Biology · doi:10.1038/s42003-025-07457-6 · Cited by 8 · see citing works
Self-citationBile Acids Alter the Autophagy and Mitogenesis in Skeletal Muscle Cells
Tacchi, F., Orozco-Aguilar, J., Valero‐Breton, M., & Cabello‐Verrugio, C. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-26163-3_10 · Cited by 5 · see citing works
Ma, D., Liu, Y., Zhao, J., & Li, Q. (2026) · Foods · doi:10.3390/foods15071162 · Cited by 2 · see citing works
Peroxisome inter-organelle cooperation in Drosophila
Cheng, A. Y., & Simmonds, A. J. (2024) · Genome · doi:10.1139/gen-2024-0082 · Cited by 2 · see citing works
Mitochondrial quality control in exercise-mitigated muscular atrophy
Fan, J., Wen, X., Duan, X., Zhu, X., Bai, J., & Zhang, T. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102074 · Cited by 2 · see citing works
An Evolutionarily Conserved Regulatory Pathway of Muscle Mitochondrial Network OrganizationPreprint
Katti, P., Ajayi, P. T., Aponte, A. M., Bleck, C. K. E., & Glancy, B. C. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.30.462204 · Cited by 2 · see citing works
n-3 Polyunsaturated fatty acids improve sarcopenia by mitochondrial quality control
Bian, D., Su, S., Cheng, X., Shi, Y., Wang, X., & Yan, Y. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.107221 · Cited by 1 · see citing works
Chen, Q., Chang, Y.-L., Hung, M.-W., Lee, P., Hsin, C., & Lin, Y. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1761278 · Cited by 1 · see citing works
Self-citationPan, Y., Liu, P., Li, S., Li, B., Li, Y., & Ma, L. (2024) · Figshare · doi:10.6084/m9.figshare.26565630
Matsui, H., Chbihi, Z. M., Mashni, R., Hachem, H., Snider, S., & Sujkowski, A. L. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1836341
Zhao, H., & Chen, M. (2026) · Biology · doi:10.3390/biology15151240
Kim, S., Noh, S. G., Ji, M., Chen, K., Kuchel, G. A., Al‐Naggar, I. M., & Kwon, O. S. (2026) · GeroScience · doi:10.1007/s11357-026-02515-1
- Authors
- Lee, T., Chen, P., Su, M. P., Li, J., Chang, Y., Liu, R., Juan, H., Yang, J., Chan, S., Tsai, Y., von Stockum, S., Ziviani, E., Kamikouchi, A., Wang, H., & Chen, C.
- Affiliations
- National Health Research Institutes (TW)
- Nagoya University (JP)
- National Taiwan University (TW)
- National Yang Ming Chiao Tung University (TW)
- Tunghai University (TW)
- Department of Biology University of Padova Padova Italy
- University of Padua (IT)
- National Tsing Hua University (TW)
- Corresponding author
- Chen, Chun‐Hong
- ORCID
- Venue
- Aging Cell
- Publisher
- Wiley
- Published
- 2021-06
- Volume
- 20
- Issue
- 6
- Pages
- e13379-e13379
- ISSN
- 1474-9718 (ISSN-L)
- 1474-9726
- PMC
- PMC8208795
- OpenAlex
- W3165819898
- Cited by
- 27
- References
- 70
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 5 · 2023: 6 · 2022: 3 · 2021: 3
- FWCI
- 1.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Aging Cell (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- Funders
- Academia Sinica
- National Health Research Institutes (08A1-MRGP12-035, NHRI-08A1-MRGP12-035)
- Japan Society for the Promotion of Science (20F20386, 20H03355)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- Fis1, mitochondrial fission, mitochondrial dynamics, skeletal muscle aging, proteostasis, mitochondrial dysfunction, oxidative stress, reactive oxygen species, ubiquitinated proteins, mitochondrial myopathy, flight performance, lifespan, Drosophila melanogaster
- MeSH terms
- Proteostasis, Aging, Animals, Drosophila melanogaster, Membrane Proteins, Muscle, Skeletal, Mitochondrial Proteins
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