A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
Open accessAbstract
The last decade has been marked by tremendous progress in our understanding of the cell biology of mitochondria, with the identification of molecules and mechanisms that regulate their fusion, fission, motility, and the architectural transitions within the inner membrane. More importantly, the manipulation of these machineries in tissues has provided links between mitochondrial dynamics and physiology. Indeed, just as the proteins required for fusion and fission were identified, they were quickly linked to both rare and common human diseases. This highlighted the critical importance of this emerging field to medicine, with new hopes of finding drugable targets for numerous pathologies, from neurodegenerative diseases to inflammation and cancer. In the midst of these exciting new discoveries, an unexpected new aspect of mitochondrial cell biology has been uncovered; the generation of small vesicular carriers that transport mitochondrial proteins and lipids to other intracellular organelles. These mitochondrial-derived vesicles (MDVs) were first found to transport a mitochondrial outer membrane protein MAPL to a subpopulation of peroxisomes. However, other MDVs did not target peroxisomes and instead fused with the late endosome, or multivesicular body. The Parkinson's disease-associated proteins Vps35, Parkin, and PINK1 are involved in the biogenesis of a subset of these MDVs, linking this novel trafficking pathway to human disease. In this review, we outline what has been learned about the mechanisms and functional importance of MDV transport and speculate on the greater impact of these pathways in cellular physiology.
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?
Mitochondrial-derived vesicles (MDVs) are a novel way that eliminates damaged mitochondria alternatively to mitophagy.
“Notably, mitochondrial-derived vesicles (MDVs) have also been identified as a novel way that eliminates damaged mitochondria alternatively of mitophagy (99).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [99]
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
Extracellular vesicles: Exosomes, microvesicles, and friends
Raposo, G., & Stoorvogel, W. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211138 · Cited by 8,099 · 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
Circulating mitochondrial DAMPs cause inflammatory responses to injury
Zhang, Q., Raoof, M., Chen, Y., Sumi, Y., Sursal, T., Junger, W., Brohi, K., Itagaki, K., & Hauser, C. J. (2010) · Nature · doi:10.1038/nature08780 · Cited by 3,812 · 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
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · 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
α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
Burré, J., Sharma, M., Tsetsenis, T., Buchman, V. L., Etherton, M. R., & Südhof, T. C. (2010) · Science · doi:10.1126/science.1195227 · Cited by 1,817 · 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
Biological Functions and Biogenesis of Secreted Bacterial Outer Membrane Vesicles
Kulp, A., & Kuehn, M. J. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073413 · Cited by 1,540 · see citing works
Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485 · 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
Self-citationMitochondrial 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
Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
Kozak, M. (1983) · Microbiological Reviews · doi:10.1128/mr.47.1.1-45.1983 · Cited by 1,278 · see citing works
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works
Mitochondrial DNA that escapes from autophagy causes inflammation and heart failure
Oka, T., Hikoso, S., Yamaguchi, O., Taneike, M., Takeda, T., Tamai, T., Oyabu, J., Murakawa, T., Nakayama, H., Nishida, K., et al. (2012) · Nature · doi:10.1038/nature10992 · Cited by 1,201 · see citing works
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115 · see citing works
Devi, L., Raghavendran, V., Prabhu, B. M., Avadhani, N. G., & Anandatheerthavarada, H. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710012200 · Cited by 1,087 · see citing works
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,087 · see citing works
Functions of plasmalogen lipids in health and disease
Braverman, N. E., & Moser, A. B. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.05.008 · Cited by 1,082 · see citing works
A mitochondrial specific stress response in mammalian cells
Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · 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
Endoplasmic reticulum-mitochondria contacts: Function of the junction
Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993 · see citing works
α-Synuclein Cooperates with CSPα in Preventing Neurodegeneration
Chandra, S. S., Gallardo, G., Fernández‐Chacón, R., Schlüter, O. M., & Südhof, T. C. (2005) · Cell · doi:10.1016/j.cell.2005.09.028 · Cited by 967 · 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
Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis
Takahashi, Y., Coppola, D., Matsushita, N., Cualing, H. D., Sun, M., Sato, Y., Liang, C., Jung, J. U., Cheng, J. Q., Mul, J. J., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1634 · Cited by 928 · see citing works
Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons
Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913 · 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
Horvath, S. E., & Daum, G. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.07.002 · Cited by 906 · see citing works
A Mutation in VPS35, Encoding a Subunit of the Retromer Complex, Causes Late-Onset Parkinson Disease
Zimprich, A. A., Benet‐Pagès, A., Struhal, W., Graf, E., Eck, S. H., Offman, M. N., Haubenberger, D., Spielberger, S., Schulte, E. C., Lichtner, P., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.008 · Cited by 885 · see citing works
VPS35 Mutations in Parkinson Disease
Vilariño‐Güell, C., Wider, C. W., Ross, O. A., Dächsel, J. C., Kachergus, J. M., Lincoln, S., Soto‐Ortolaza, A. I., Cobb, S. A., Wilhoite, G. J., Bacon, J. A., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.001 · Cited by 877 · see citing works
Zhong, Q., Gao, W., Du, F., & Wang, X. (2005) · Cell · doi:10.1016/j.cell.2005.06.009 · Cited by 844 · see citing works
Li, W., Bengtson, M. H., Ulbrich, A., Matsuda, A., Reddy, V. A., Orth, A. P., Chanda, S. K., Batalov, S., & Joazeiro, C. A. P. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001487 · Cited by 839 · see citing works
Casari, G., Fusco, M. D., Ciarmatori, S., Zeviani, M., Mora, M., Fernández‐Silva, P., Michele, G. D., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 826 · 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
Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates
Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 798 · see citing works
Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.-W., Yang, L., Beal, M. F., Vogel, H., & Lu, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602493103 · Cited by 798 · see citing works
Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769 · see citing works
Deatherage, B. L., & Cookson, B. T. (2012) · Infection and Immunity · doi:10.1128/iai.06014-11 · Cited by 765 · see citing works
A Membrane Coat Complex Essential for Endosome-to-Golgi Retrograde Transport in Yeast
Seaman, M. N. J., McCaffery, J. M., & Emr, S. D. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.3.665 · Cited by 756 · 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
Self-citationMcLelland, 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
Self-citationMitochondrial 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
“During import, PINK1 is first cleaved by the matrix processing peptidases and PARL (Jin et al, 2010; Greene et al, 2012); however, almost all of the cleaved PINK1 is then released from the import channel and degraded in the cytosol through the N-end rule proteolytic pathway (Kondapalli et al, 2012;…”
BackgroundInfluentialSelf-citationLazarou, 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
PINK1 is degraded through the N-end rule pathway
Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 669 · see citing works
Dnm1 forms spirals that are structurally tailored to fit mitochondria
Ingerman, E., Perkins, E. M., Marino, M., Mears, J. A., McCaffery, J. M., Hinshaw, J. E., & Nunnari, J. (2005) · Journal of Cell Biology · doi:10.1083/jcb.200506078 · Cited by 621 · see citing works
Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R., & Bonifacino, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200312055 · Cited by 601 · see citing works
Cargo-Selected Transport from the Mitochondria to Peroxisomes Is Mediated by Vesicular Carriers
Neuspiel, M., Schauss, A. C., Braschi, E., Zunino, R., Rippstein, P. U., Rachubinski, R. A., Andrade-Navarro, M. A., & McBride, H. M. (2008) · Current Biology · doi:10.1016/j.cub.2007.12.038 · Cited by 592 · see citing works
Self-citationNakamura, K., Nemani, V., Azarbal, F., Skibinski, G., Levy, J. M., Egami, K., Munishkina, L. A., Zhang, J., Gardner, B. M., Wakabayashi, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213538 · Cited by 590 · 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 · see citing works
Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles.
Kozak, M. (1983) · Microbiological Reviews · doi:10.1128/mmbr.47.1.1-45.1983 · Cited by 569 · see citing works
Quasi‐synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
Csordás, G., Thomas, A. P., & Hajnóczky, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.96 · Cited by 536 · see citing works
Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 517 · see citing works
Proteomics, transcriptomics and lipidomics of exosomes and ectosomes
Choi, D., Kim, D., Kim, Y., & Gho, Y. S. (2013) · PROTEOMICS · doi:10.1002/pmic.201200329 · Cited by 513 · 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
α-Synuclein Is Localized to Mitochondria-Associated ER Membranes
Guardia-Laguarta, C., Area-Gómez, E., Rüb, C., Liu, Y.-H., Magrané, J., Becker, D., Voos, W., Schon, E., & Przedborski, S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2507-13.2014 · Cited by 489 · see citing works
A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis
Choi, S., Huang, P., Jenkins, G. M., Chan, D. C., Schiller, J., & Frohman, M. A. (2006) · Nature Cell Biology · doi:10.1038/ncb1487 · Cited by 480 · 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
Assembly-dependent endocytosis and clearance of extracellular a-synuclein
Lee, H.-J., Suk, J.-E., Bae, E.-J., Lee, J.-H., Paik, S. R., & Lee, S.-J. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.01.017 · Cited by 470 · see citing works
Advances in the genetics of Parkinson disease
Trinh, J., & Farrer, M. J. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.132 · Cited by 465 · see citing works
Contribution of the Endoplasmic Reticulum to Peroxisome Formation
Hoepfner, D., Schildknegt, D., Braakman, I., Philippsen, P., & Tabak, H. F. (2005) · Cell · doi:10.1016/j.cell.2005.04.025 · Cited by 463 · see citing works
The retromer complex – endosomal protein recycling and beyond
Seaman, M. N. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.103440 · Cited by 455 · see citing works
Clearance of α-Synuclein Oligomeric Intermediates via the Lysosomal Degradation Pathway
Lee, H.-J., Khoshaghideh, F., Patel, S., & Lee, S.-J. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3809-03.2004 · Cited by 445 · see citing works
Unconventional secretion of Acb1 is mediated by autophagosomes
Duran, J. M., Anjard, C., Stefan, C., Loomis, W. F., & Malhotra, V. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911154 · Cited by 433 · see citing works
Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works
Nolden, M., Ehses, S., Koppen, M., Bernacchia, A., Rugarli, E. I., & Langer, T. (2005) · Cell · doi:10.1016/j.cell.2005.08.003 · Cited by 398 · see citing works
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
Kim, Y. S., Park, J., Kim, S., Song, S., Kwon, S., Lee, S., Kitada, T., Kim, J., & Chung, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.104 · Cited by 389 · see citing works
Dynamin-like protein 1 is involved in peroxisomal fission
Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M. A., & Schrader, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211761200 · Cited by 374 · see citing works
Fallon, L., Bélanger, C., Corera, A. T., Kontogiannea, M., Regan‐Klapisz, E., Moreau, F., Voortman, J., Haber, M., Rouleau, G., Thorarinsdottir, T., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1441 · Cited by 357 · see citing works
Self-citationDiao, J., Burré, J., Vivona, S., Cipriano, D. J., Sharma, M., Kyoung, M., Südhof, T. C., & Brünger, A. T. (2013) · eLife · doi:10.7554/elife.00592 · Cited by 351 · see citing works
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 · see citing works
Self-citationSorting nexins provide diversity for retromer-dependent trafficking events
Cullen, P. J., & Korswagen, H. C. (2011) · Nature Cell Biology · doi:10.1038/ncb2374 · Cited by 348 · see citing works
Soubannier, V., Rippstein, P. U., Kaufman, B. A., Shoubridge, E. A., & McBride, H. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052830 · Cited by 346 · see citing works
Self-citationMutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28
Bella, D. D., Lazzaro, F., Brusco, A., Plumari, M., Battaglia, G. S., Pastore, A., Finardi, A., Cagnoli, C., Tempia, F., Frontali, M., et al. (2010) · Nature Genetics · doi:10.1038/ng.544 · Cited by 345 · see citing works
Kim, P. K., Mullen, R. T., Schümann, U., & Lippincott‐Schwartz, J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601036 · Cited by 344 · see citing works
Clearance and deposition of extracellular α-synuclein aggregates in microglia
Lee, H.-J., Suk, J.-E., Bae, E.-J., & Lee, S.-J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.05.045 · Cited by 343 · see citing works
Manjithaya, R. R., Anjard, C., Loomis, W. F., & Subramani, S. E. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911149 · Cited by 337 · see citing works
Huang, H., Gao, Q., Peng, X., Choi, S., Sarma, K., Ren, H., Morris, A. J., & Frohman, M. A. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.01.004 · Cited by 323 · see citing works
Sacksteder, K. A., Jones, J. M., South, S. T., Li, X., Liu, Y., & Gould, S. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.931 · Cited by 317 · see citing works
Protein selection and export via outer membrane vesicles
Bonnington, K. E., & Kuehn, M. J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.12.011 · Cited by 309 · see citing works
Vps35 Mediates Vesicle Transport between the Mitochondria and Peroxisomes
Braschi, E., Goyon, V., Zunino, R., Mohanty, A., Xu, L., & McBride, H. M. (2010) · Current Biology · doi:10.1016/j.cub.2010.05.066 · Cited by 308 · see citing works
Self-citationA role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A., & Schrader, M. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-02-0159 · Cited by 308 · see citing works
Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
Yamano, K., Fogel, A. I., Wang, C., van der Bliek, A. M., & Youle, R. J. (2014) · eLife · doi:10.7554/elife.01612 · Cited by 307 · see citing works
Extracellular α-synuclein—a novel and crucial factor in Lewy body diseases
Lee, H.-J., Bae, E.-J., & Lee, S. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.275 · Cited by 304 · see citing works
A Stress-Responsive System for Mitochondrial Protein Degradation
Heo, J.-M., Livnat-Levanon, N., Taylor, E. B., Jones, K. T., Dephoure, N., Ring, J., Xie, J., Brodsky, J. L., Madeo, F., Gygi, S. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.021 · Cited by 304 · see citing works
Atorino, L., Silvestri, L., Koppen, M., Cassina, L., Ballabio, A., Marconi, R., Langer, T., & Casari, G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304112 · Cited by 283 · see citing works
A role for lipid droplets in inter‐membrane lipid traffic
Zehmer, J. K., Huang, Y., Gong, P., Pu, J., Anderson, R. G. W., & Liu, P. (2009) · PROTEOMICS · doi:10.1002/pmic.200800584 · Cited by 282 · see citing works
Mitochondrial iron–sulfur protein biogenesis and human disease
Stehling, O., Wilbrecht, C., & Lill, R. (2014) · Biochimie · doi:10.1016/j.biochi.2014.01.010 · Cited by 272 · see citing works
Direct interorganellar transfer of iron from endosome to mitochondrion
Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 266 · see citing works
Endophilin B1 is required for the maintenance of mitochondrial morphology
Karbowski, M., Jeong, S., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200407046 · Cited by 264 · see citing works
Shiao, Y., Lupo, G., & Vance, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11190 · Cited by 261 · see citing works
Absence of nigral degeneration in aged parkin/DJ‐1/PINK1 triple knockout mice
Kitada, T., Tong, Y., Gautier, C., & Shen, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06350.x · Cited by 260 · see citing works
The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
Xu, S., Peng, G., Wang, Y., Fang, S., & Karbowski, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0748 · Cited by 243 · see citing works
Kong, S. M. Y., Chan, B. K. K., Park, J., Hill, K. J., Aitken, J. B., Cottle, L., Farghaian, H., Cole, A. R., Lay, P. A., Sue, C. M., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu099 · Cited by 233 · see citing works
Rojas, R., Kametaka, S., Haft, C. R., & Bonifacino, J. S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00156-06 · Cited by 230 · see citing works
Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics
Alto, N. M., Soderling, J. A., & Scott, J. D. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204081 · Cited by 222 · see citing works
Baumgart, E., Vanhorebeek, I., Grabenbauer, M., Borgers, M., Declercq, P. E., Fahimi, H. D., & Baes, M. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62534-5 · Cited by 210 · see citing works
Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation
Iguchi, M., Kujuro, Y., Okatsu, K., Koyano, F., Kosako, H., Kimura, M., Suzuki, N., Uchiyama, S., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.467530 · Cited by 209 · see citing works
THE SYNTHESIS AND TURNOVER OF RAT LIVER PEROXISOMES
Lazarow, P. B., & Duve, C. D. (1973) · The Journal of Cell Biology · doi:10.1083/jcb.59.2.507 · Cited by 197 · see citing works
Caza, T. N., Fernandez, D. R., Talaber, G., Oaks, Z., Haas, M., Madaio, M. P., Lai, Z.-W., Miklossy, G., Singh, R. R., Chudakov, D. M., et al. (2014) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2013-203794 · Cited by 193 · see citing works
Loss of Bif-1 Suppresses Bax/Bak Conformational Change and Mitochondrial Apoptosis
Takahashi, Y., Karbowski, M., Yamaguchi, H., Kazi, A., Wu, J., Sebti, S. M., Youle, R. J., & Wang, H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9369-9382.2005 · Cited by 190 · see citing works
Mitochondrial translocation of α-synuclein is promoted by intracellular acidification
Cole, N. B., DiEuliis, D., Leo, P., Mitchell, D. C., & Nussbaum, R. L. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.03.012 · Cited by 183 · see citing works
THE SYNTHESIS AND TURNOVER OF RAT LIVER PEROXISOMES
Leighton, F., Poole, B., Lazarow, P. B., & Duve, C. D. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.41.2.521 · Cited by 180 · see citing works
Unconventional Secretion, Unconventional Solutions
Zhang, M., & Schekman, R. W. (2013) · Science · doi:10.1126/science.1234740 · Cited by 179 · see citing works
The Minimal Proteome in the Reduced Mitochondrion of the Parasitic Protist Giardia intestinalis
Jedelský, P. L., Doležal, P., Rada, P., Pyrih, J., Šmíd, O., Hrdý, I., Šedinová, M., Marcinčiková, M., Voleman, L., Perry, A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017285 · Cited by 178 · see citing works
Rab32 Modulates Apoptosis Onset and Mitochondria-associated Membrane (MAM) Properties
Bui, M., Gilady, S. Y., Fitzsimmons, R., Benson, M. D., Lynes, E. M., Gesson, K., Alto, N. M., Strack, S., Scott, J. D., & Simmen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101584 · Cited by 177 · see citing works
Origin and evolution of the peroxisomal proteome
Gabaldón, T., Snel, ., van Zimmeren, F., Hemrika, W., Tabak, H. F., & Huynen, M. A. (2006) · Biology Direct · doi:10.1186/1745-6150-1-8 · Cited by 176 · 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
Wurm, C. A., Neumann, D., Lauterbach, M. A., Harke, B., Egner, A., Hell, S. W., & Jakobs, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107553108 · Cited by 173 · see citing works
Selective escape of proteins from the mitochondria during mitophagy
Saita, S., Shirane, M., & Nakayama, K. I. (2013) · Nature Communications · doi:10.1038/ncomms2400 · Cited by 161 · see citing works
Methylation pattern of mouse mitochondrial DNA
Pollack, Y., Kasir, J., Shemer, R., Metzger, S., & Moshe Szyf, A. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.12.4811 · Cited by 161 · see citing works
Exosomes from Myeloid-Derived Suppressor Cells Carry Biologically Active Proteins
Burke, M. C., Choksawangkarn, W., Edwards, N. J., Ostrand‐Rosenberg, S., & Fenselau, C. (2013) · Journal of Proteome Research · doi:10.1021/pr400879c · Cited by 157 · see citing works
Inhibitors of Copi and Copii Do Not Block PEX3-Mediated Peroxisome Synthesis
South, S. T., Sacksteder, K. A., Li, X., Liu, Y., & Gould, S. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.7.1345 · Cited by 150 · 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
Trempe, J., Chen, C. X. ‐., Grenier, K., Matta‐Camacho, E., Kozlov, G., McPherson, P. S., Gehring, K., & Fon, E. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.021 · Cited by 138 · see citing works
Self-citationA vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum
Lam, S. K., Yoda, N., & Schekman, R. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013397107 · Cited by 136 · see citing works
Isenmann, S., Khew‐Goodall, Y., Gamble, J. R., et al. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.7.1649 · Cited by 131 · see citing works
Normal and disordered reticulocyte maturation
Ney, P. A. (2011) · Current Opinion in Hematology · doi:10.1097/moh.0b013e328345213e · Cited by 129 · see citing works
BH3‐ligand regulates access of MCL‐1 to its E3 ligase
Warr, M. R., Acoca, S., Liu, Z., et al. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.09.028 · Cited by 120 · 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
Zhang, A., Sheftel, A. D., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-06-2226 · Cited by 119 · see citing works
Phosphoinositides and vesicular membrane traffic
Mayinger, P. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.01.002 · Cited by 119 · see citing works
Structure of Vps26B and Mapping of its Interaction with the Retromer Protein Complex
Collins, B. M., Norwood, S. J., Kerr, M. C., Mahony, D., Seaman, M. N. J., Teasdale, R. D., & Owen, D. J. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00688.x · Cited by 118 · see citing works
SH3GLB, a New Endophilin-Related Protein Family Featuring an SH3 Domain
Pierrat, B., Simonen, M., Cueto, M. A., Mestan, J., Ferrigno, P. K., & Heim, J. (2001) · Genomics · doi:10.1006/geno.2000.6378 · Cited by 113 · see citing works
Interaction of α-synuclein with vesicles that mimic mitochondrial membranes
Zigoneanu, I. G., Yang, Y. J., Krois, A. S., Haque, M. E., & Pielak, G. J. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.024 · 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
AAA proteases in mitochondria: diverse functions of membrane-bound proteolytic machines
Tatsuta, T., & Langer, T. (2009) · Research in Microbiology · doi:10.1016/j.resmic.2009.09.005 · Cited by 95 · see citing works
Yonekawa, S., Furuno, A., Baba, T., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103283108 · Cited by 93 · see citing works
Aging, Age-Related Diseases and Peroxisomes
Fransen, M., Nordgren, M., Wang, B., Apanasets, O., & Veldhoven, P. P. V. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-6889-5_3 · Cited by 90 · see citing works
Phospholipase D in endocytosis and endosomal recycling pathways
Donaldson, J. G. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.05.011 · Cited by 90 · see citing works
Insights into the mechanisms of sterol transport between organelles
Mesmin, B., Antonny, B., & Drin, G. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1247-3 · Cited by 88 · see citing works
GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth
Zhang, B., Huang, J., Li, H., Liu, T., Wang, Y., Waterman, P. M., Mao, A., Xu, L., Zhai, Z., Liu, D., et al. (2008) · Cell Research · doi:10.1038/cr.2008.75 · Cited by 84 · see citing works
Emerging roles of mitochondria in the evolution, biogenesis, and function of peroxisomes
Mohanty, A., & McBride, H. M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00268 · Cited by 76 · see citing works
Self-citationNemoto, Y., Wenk, M. R., Watanabe, M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106404200 · 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
Targeting of hFis1 to Peroxisomes Is Mediated by Pex19p
Delille, H. K., & Schrader, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803332200 · Cited by 72 · see citing works
Schrader, M., Baumgart‐Vogt, E., Völkl, A., & Fahimi, H. D. (1994) · PubMed · Cited by 69 · see citing works
The Role of the Endoplasmic Reticulum in Peroxisome BiogenesisPreprint
Dimitrov, L., Lam, S. K., & Schekman, R. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013243 · Cited by 69 · see citing works
Mitochondrial vesicles: an ancient process providing new links to peroxisomes
Andrade-Navarro, M. A., Sánchez‐Pulido, L., & McBride, H. M. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.04.005 · Cited by 68 · see citing works
Self-citationE3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53
Jung, J. H., Bae, S., Lee, J. Y., Woo, S. R., Cha, H. J., Yoon, Y., Suh, K.-S., Lee, S.-J., Park, I.-C., Jin, Y.-W., et al. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.57 · Cited by 55 · see citing works
Pex3p‐dependent peroxisomal biogenesis initiates in the endoplasmic reticulum of human fibroblasts
Toro, A., Araya, C. A. G., Córdova, G., Arredondo, C., Cárdenas, H. G., Moreno, R. E., Venegas, A., Koenig, C. S., Cancino, J., González, A., et al. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22210 · Cited by 54 · see citing works
Talabér, G., Miklóssy, G., Oaks, Z., Liu, Y., Tooze, S. A., Chudakov, D. M., Bánki, K., & Perl, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084392 · Cited by 52 · see citing works
De novo synthesis of peroxisomes upon mitochondrial targeting of Pex3p
Rucktäschel, R., Halbach, A., Girzalsky, W., Rottensteiner, H., & Erdmann, R. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.06.012 · Cited by 41 · see citing works
Landry, M.-C., Champagne, C., Boulanger, M., Jetté, A., Fuchs, M., Dziengelewski, C., & Lavoie, J. N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516351 · Cited by 39 · see citing works
Formation of phosphatidic acid in stressed mitochondria
Yurkova, I. L., Stuckert, F., Kisel, M. A., Шадыро, О. И., Arnhold, J., & Hüster, D. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.09.007 · Cited by 33 · see citing works
Peroxisomes: The neuropathological consequences of peroxisomal dysfunction in the developing brain
Barry, D., & O’Keeffe, G. W. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.019 · Cited by 22 · see citing works
Powers, J. M. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:16:2-3:285 · Cited by 19 · see citing works
Reconsidering ideas regarding the evolution of peroxisomes: the case for a mitochondrial connection
Speijer, D. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1507-x · Cited by 16 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works
The mitochondrial basis of aging
Sun, N., Youle, R. J., & Finkel, T. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.028 · Cited by 1,441 · see citing works
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416 · see citing works
Cargo recognition and degradation by selective autophagy
Gatica, D., Lahiri, V., & Klionsky, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0037-z · Cited by 1,067 · see citing works
BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis
McArthur, K., Whitehead, L. W., Heddleston, J. M., Li, L., Padman, B. S., Oorschot, V., Geoghegan, N. D., Chappaz, S., Davidson, S., San Chin, H., et al. (2018) · Science · doi:10.1126/science.aao6047 · Cited by 1,072 · see citing works
Mitochondria in the Regulation of Innate and Adaptive Immunity
Weinberg, S. E., Sena, L. A., & Chandel, N. S. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.002 · Cited by 960 · 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
Microglia monitor and protect neuronal function through specialized somatic purinergic junctions
Cserép, C., Pósfai, B., Lénárt, N., Fekete, R., László, Z. I., Lele, Z., Orsolits, B., Molnár, G., Heindl, S., Schwarcz, A. D., et al. (2020) · Science · doi:10.1126/science.aax6752 · Cited by 684 · see citing works
Parkinson’s Disease-Related Proteins PINK1 and Parkin Repress Mitochondrial Antigen Presentation
Matheoud, D., Sugiura, A., Bellemare-Pelletier, A., Laplante, A., Rondeau, C., Chemali, M., Fazel, A., Bergeron, J. J., Trudeau, L.-E., Burelle, Y., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.039 · Cited by 582 · see citing works
Self-citationThe potential of endurance exercise-derived exosomes to treat metabolic diseases
Safdar, A., Saleem, A., & Tarnopolsky, M. A. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.76 · Cited by 463 · see citing works
Mechanisms of Selective Autophagy
Lamark, T., & Johansen, T. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120219-035530 · Cited by 429 · see citing works
Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes
Sugiura, A., Mattie, S., Prudent, J., & McBride, H. M. (2017) · Nature · doi:10.1038/nature21375 · Cited by 386 · see citing works
Self-citationThe three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications
Durcan, T. M., & Fon, E. A. (2015) · Genes & Development · doi:10.1101/gad.262758.115 · Cited by 400 · see citing works
Self-citationTodkar, K., Chikhi, L., Desjardins, V., El-Mortada, F., Pépin, G., & Germain, M. (2021) · Nature Communications · doi:10.1038/s41467-021-21984-w · Cited by 382 · see citing works
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351 · see citing works
“The physiological role of these MUL1-positive MDVs has been the subject of debate [74].”
BackgroundThe role of mitochondria in aging
Jang, J. Y., Blum, A., Liu, J., & Finkel, T. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120842 · Cited by 358 · see citing works
Mitophagy in neurodegeneration and aging
Fivenson, E. M., Lautrup, S., Sun, N., Scheibye-Knudsen, M., Stevnsner, T., Nilsen, H., Bohr, V. A., & Fang, E. F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.02.007 · Cited by 364 · 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
Shaping Neuronal Fate: Functional Heterogeneity of Direct Microglia-Neuron Interactions
Cserép, C., Pósfai, B., & Dénes, Á. (2021) · Neuron · doi:10.1016/j.neuron.2020.11.007 · Cited by 256 · see citing works
Abuaita, B. H., Schultz, T. L., & O’Riordan, M. X. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.10.005 · Cited by 223 · see citing works
Exosomes as Mediators of the Systemic Adaptations to Endurance Exercise
Safdar, A., & Tarnopolsky, M. A. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029827 · Cited by 203 · see citing works
Antibiotic-induced release of small extracellular vesicles (exosomes) with surface-associated DNA
Németh, A., Orgovan, N., Sódar, B. W., Osteikoetxea, X., Pálóczi, K., Szabó-Taylor, K. É., Vukman, K. V., Kittel, Á., Turiák, L., Wiener, Z., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08392-1 · Cited by 146 · see citing works
Autophagy in neurodegeneration: New insights underpinning therapy for neurological diseases
Corti, O., Blomgren, K., Poletti, A., & Beart, P. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15002 · Cited by 141 · see citing works
Forms of extracellular mitochondria and their impact in health
Miliotis, S., Nicolalde, B., Ortega, M., Yepez, J., & Caicedo, A. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.02.002 · Cited by 138 · see citing works
Skeletal Muscle-Released Extracellular Vesicles: State of the Art
Rome, S., Forterre, A., Mizgier, M. L., & Bouzakri, K. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00929 · Cited by 139 · see citing works
Vincent, A. E., Turnbull, D. M., Eisner, V., Hajnóczky, G., & Picard, M. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.08.009 · Cited by 135 · see citing works
Cholesterol impairs autophagy-mediated clearance of amyloid beta while promoting its secretion
Barbero-Camps, E., Roca-Agujetas, V., Bartolessis, I., de Dios, C., Fernández-Checa, J. C., Marí, M., Morales, A., Hartmann, T., & Colell, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1438807 · Cited by 125 · see citing works
Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79 · see citing works
Faizan, M. I., Chaudhuri, R., Sagar, S., Albogami, S., Chaudhary, N., Azmi, I., Akhtar, A., Ali, S. M., Kumar, R., Iqbal, J., et al. (2022) · Cells · doi:10.3390/cells11192969 · Cited by 61 · see citing works
Extracellular Vesicles as Novel Diagnostic and Prognostic Biomarkers for Parkinson’s Disease
Leggio, L., Paternò, G., Vivarelli, S., Falzone, G. G., Giachino, C., Marchetti, B., & Iraci, N. (2021) · Aging and disease · doi:10.14336/ad.2021.0527 · Cited by 55 · 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
“Notably, mitochondrial-derived vesicles (MDVs) have also been identified as a novel way that eliminates damaged mitochondria alternatively of mitophagy (99).”
BackgroundEtiology of type 2 diabetes and Alzheimer’s disease: Exploring the mitochondria
Silzer, T. K., & Phillips, N. R. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.04.004 · Cited by 53 · see citing works
Lin, T.-K., Lin, K.-J., Lin, K.-L., Liou, C.-W., Chen, S.-D., Chuang, Y.-C., Wang, P.-W., Chuang, J.-H., & Wang, T.-J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607392 · Cited by 19 · see citing works
- Authors
- Sugiura, A., McLelland, G., Fon, E. A., & McBride, H. M.
- Affiliations
- McGill University (CA)
- Corresponding author
- McBride, Heidi M
- Venue
- The EMBO Journal
- Published
- 2014-08-08
- Volume
- 33
- Issue
- 19
- Pages
- 2142-2156
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC4282503
- OpenAlex
- W2110054105
- Cited by
- 862
- References
- 155
- Citations by year
- 2026: 64 · 2025: 65 · 2024: 104 · 2023: 79 · 2022: 95 · 2021: 95 · 2020: 82 · 2019: 58 · 2018: 62 · 2017: 61 · 2016: 50 · 2015: 41 · 2014: 5
- FWCI
- 6.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- Heart and Stroke Foundation of Ontario
- Topics
- Health Sciences › Medicine › Epidemiology › 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 › Cell Biology › Cellular transport and secretion
- Keywords
- mitochondrial-derived vesicles, mitochondrial quality control, MAPL, peroxisomes, multivesicular bodies, late endosomes, Parkinson's disease, VPS35, Parkin, PINK1, mitochondrial dynamics, mitochondrial fission and fusion
- MeSH terms
- Animals, Humans, Mitochondria, Organelles, Transport Vesicles, 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