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During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Open accessAbstract
A plethora of cellular processes, including apoptosis, depend on regulated changes in mitochondrial shape and ultrastructure. The role of mitochondria and of their morphology during autophagy, a bulk degradation and recycling process of eukaryotic cells' constituents, is not well understood. Here we show that mitochondrial morphology determines the cellular response to macroautophagy. When autophagy is triggered, mitochondria elongate in vitro and in vivo. During starvation, cellular cyclic AMP levels increase and protein kinase A (PKA) is activated. PKA in turn phosphorylates the pro-fission dynamin-related protein 1 (DRP1), which is therefore retained in the cytoplasm, leading to unopposed mitochondrial fusion. Elongated mitochondria are spared from autophagic degradation, possess more cristae, increased levels of dimerization and activity of ATP synthase, and maintain ATP production. Conversely, when elongation is genetically or pharmacologically blocked, mitochondria consume ATP, precipitating starvation-induced death. Thus, regulated changes in mitochondrial morphology determine the fate of the cell during autophagy.
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“Twelve h of fasting in mice may be sufficient to trigger autophagy in muscle, 639,640 but the appropriate time should be determined empirically.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [639]
In the citing paper
“This process enables the redistribution of energy in the form of mitochondrial potential, metabolites, proteins, and mtDNA, improving calcium handling, and ATP synthesis [24, 54–57].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [55]
In the citing paper
“This is corroborated by our findings that either Mdivi-1 (mitophagy inhibitor) (49) or rotenone (increasing mtROS generation) (35) induced perinuclear accumulation of damaged mitochondria and cellular senescence.”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [49]
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“These results are in agreement with the previous reports showing impaired mitophagy occurring during mitochondrial elongation (49).”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [49]
In the citing paper
“This is corroborated by our findings that either Mdivi-1 (mitophagy inhibitor) (49) or rotenone (increasing mtROS generation) (35) induced perinuclear accumulation of damaged mitochondria and cellular senescence.”
From Impaired mitophagy leads to cigarette smoke stress‐induced cellular senescence: implications for chronic obstructive pulmonary disease (2015) · cites this paper as [49]
In the citing paper
“Cells under a well-fed condition maintain their mitochondria in a separated (or fragmented) state, while under fasting or starved conditions, mitochondria tend to persist in a connected (or fused) state (Gomes et al, 2011).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Gomes et al, 2011
In the citing paper
“Indeed, as described below, changes in mitochondrial architecture can affect respiratory complex assembly and the proper coupling of respiration to ATP synthesis (Gomes et al, 2011).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Gomes et al, 2011
In the citing paper
“Elongated mitochondria upon fasting possess more cristae and increased levels of dimerization and activity of ATP synthase, ensuring a better coupling of fuel oxidation with ATP synthesis (Gomes et al, 2011).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Gomes et al, 2011
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Citations
Cites
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
Autophagy as a Regulated Pathway of Cellular Degradation
Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630
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
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Self-citationReactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · cited 1×
“, to the amplification of the process, in which mitochondria-derived reactive oxygen species seem to play a rol”
BackgroundDynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673
Self-citationThe importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
Li, Z., Okamoto, K.-I., Hayashi, Y., & Sheng, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.003 · Cited by 1,498
Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation
Hailey, D. W., Rambold, A. S., Satpute‐Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott‐Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,491
BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
Self-citationDisruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376
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
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300
Self-citationOrganelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188
Self-citationDephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129
Self-citationAggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
Ravikumar, B. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.9.1107 · Cited by 1,099
A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072
Self-citationIshihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066
Cribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response
Bernales, S., McDonald, K. L., & Walter, P. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040423 · Cited by 1,047
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012
Bereiter‐Hahn, J., & Vöth, M. (1994) · Microscopy Research and Technique · doi:10.1002/jemt.1070270303 · Cited by 900
Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 831
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 824
Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 818
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 796
Dynamics of mitochondrial morphology in healthy cells and during apoptosis
Karbowski, M., & Youle, R. J. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401260 · Cited by 780
Drosophila 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
BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
Danial, N. N., Gramm, C. F., Scorrano, L., Zhang, C.-Y., Krauss, S., Ranger, A. M., Robert Datta, S., Greenberg, M. E., Licklider, L. J., Lowell, B. B., et al. (2003) · Nature · doi:10.1038/nature01825 · Cited by 705
Self-citationNovel Single Chain cAMP Sensors for Receptor-induced Signal Propagation
Nikolaev, V. O., Bünemann, M., Hein, L., Hannawacker, A., & Lohse, M. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400302200 · Cited by 688
Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
Strauss, M., Hofhaus, G., Schröder, R. R., & Kühlbrandt, W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.35 · Cited by 677
Mitra, K., Wunder, C., Roysam, B., Lin, G., & Lippincott‐Schwartz, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904875106 · Cited by 652
The Adaptor Protein p62/SQSTM1 Targets Invading Bacteria to the Autophagy Pathway
Zheng, Y. T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T., & Brumell, J. H. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900441 · Cited by 616
The origin of the autophagosomal membrane
Tooze, S. A., & Yoshimori, T. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-831 · Cited by 611
The mitochondrial permeability transition initiates autophagy in rat hepatocytes
Elmore, S. P., Qian, T., Grissom, S. F., & Lemasters, J. J. (2001) · The FASEB Journal · doi:10.1096/fj.01-0206fje · Cited by 607
Control of respiration and ATP synthesis in mammalian mitochondria and cells
Brown, G. C. (1992) · Biochemical Journal · doi:10.1042/bj2840001 · Cited by 598
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 537
The Role of Autophagy in Mammalian Development: Cell Makeover Rather than Cell Death
Cecconi, F., & Levine, B. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.012 · Cited by 535
The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
Karbowski, M., Neutzner, A., & Youle, R. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611064 · Cited by 485
Mitochondrial Inner-Membrane Fusion and Crista Maintenance Requires the Dynamin-Related GTPase Mgm1
Meeusen, S., DeVay, R. M., Block, J., Cassidy-Stone, A., Wayson, S. M., McCaffery, J. M., & Nunnari, J. M. (2006) · Cell · doi:10.1016/j.cell.2006.09.021 · Cited by 474
Szabadkai, G., Simoni, A. M., Chami, M., Wieckowski, M. R., Youle, R. J., & Rizzuto, R. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.026 · Cited by 468
Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309082 · Cited by 433
MARCH‐V is a novel mitofusin 2‐ and Drp1‐binding protein able to change mitochondrial morphology
Nakamura, N., Kimura, Y. N., Tokuda, M., Honda, S., & Hirose, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400790 · Cited by 419
Sumo1 Conjugates Mitochondrial Substrates and Participates in Mitochondrial Fission
Harder, Z., Zunino, R., & McBride, H. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.02.004 · Cited by 367
Glucagon physiology and pathophysiology in the light of new advances
Unger, R. H. (1985) · Diabetologia · doi:10.1007/bf00281991 · Cited by 361
Pan, X., & Heitman, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.4874 · Cited by 350
MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
Braschi, E., Zunino, R., & McBride, H. M. (2009) · EMBO Reports · doi:10.1038/embor.2009.86 · Cited by 350
Scheckhuber, C. Q., Erjavec, N., Tinazli, A., Hamann, A., Nyström, T., & Osiewacz, H. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1524 · Cited by 344
Orchestration of lymphocyte chemotaxis by mitochondrial dynamics
Campello, S., Lacalle, R. A., Bettella, M., Mañes, S., Scorrano, L., & Viola, A. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061877 · Cited by 325
Self-citationStephan, J. S., Yeh, Y.-Y., Ramachandran, V., Deminoff, S. J., & Herman, P. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903316106 · Cited by 316
Martinou, I., Desagher, S., Eskes, R., Antonsson, B. E., André, É., Fakan, S., & Martinou, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.883 · Cited by 316
Costa, V., Giacomello, M., Hudec, R., Lopreiato, R., Ermak, G., Lim, D., Malorni, W., Davies, K. J. A., Carafoli, E., & Scorrano, L. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000102 · Cited by 293
Self-citationHigh 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 242
Self-citationBudovskaya, Y. V., Stephan, J. S., Reggiori, F., Klionsky, D. J., & Herman, P. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400272200 · Cited by 215
Roy, A. (1999) · Medical Entomology and Zoology · Cited by 169
Alirol, E., James, D. I., Huber, D., Marchetto, A., Vergani, L., Martinou, J., & Scorrano, L. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0377 · Cited by 128
Self-citationGiraud, M., Paumard, P., Soubannier, V., Vaillier, J., Arselin, G., Salin, B., Schaëffer, J., Brèthes, D., di Rago, J., & Velours, J. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00274-8 · Cited by 128
Chemiosmotic coupling: The cost of living
Rich, P. R. (2003) · Nature · doi:10.1038/421583a · Cited by 127
Selective autophagy of peroxisomes in methylotrophic yeasts.
Tuttle, D. L., Lewin, A. S., & Dunn, W. A. (1993) · PubMed · Cited by 123
Cereghetti, G. M., Costa, V., & Scorrano, L. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.61 · Cited by 121
Self-citationMavrakis, M., Lippincott‐Schwartz, J., Stratakis, C. A., & Bossis, I. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl239 · Cited by 107
Loss of Drp1 function alters OPA1 processing and changes mitochondrial membrane organization
Möpert, K., Hajek, P., Frank, S., Chen, C. I.-U., Kaufmann, J., & Santel, A. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.04.016 · Cited by 67
Slattery, M. G., Liko, D., & Heideman, W. (2007) · Eukaryotic Cell · doi:10.1128/ec.00334-07 · Cited by 62
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- de Brito, O. M. & Scorrano, L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456, 605–610 (2008). · DOI · Paper page
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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
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AMPK: guardian of metabolism and mitochondrial homeostasis
Herzig, S., & Shaw, R. J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.95 · Cited by 4,192
Guidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996
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Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674
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Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Metadata
- Authors
- Gomes, L. C., Benedetto, G. D., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- University of Geneva (CH)
- Corresponding author
- Scorrano, Luca
- Venue
- Nature Cell Biology
- Published
- 2011-04-10
- Volume
- 13
- Issue
- 5
- Pages
- 589-598
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC3088644
- OpenAlex
- W2121077787
- Cited by
- 1,735
- References
- 65
- Citations by year
- 2026: 63 · 2025: 94 · 2024: 120 · 2023: 120 · 2022: 106 · 2021: 145 · 2020: 153 · 2019: 129 · 2018: 116 · 2017: 135 · 2016: 127 · 2015: 89 · 2014: 116 · 2013: 96 · 2012: 96
- FWCI
- 80.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (118171)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- autophagy, mitochondrial morphology, mitochondrial elongation, mitochondrial fusion, Drp1, protein kinase A, cyclic AMP, starvation, ATP synthase, ATP production, mitochondrial cristae, cell viability
- MeSH terms
- Adenosine Triphosphate, Animals, Autophagy, Cell Line, Humans, Mitochondria, Cell Death, Mice
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