The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast
Open accessAbstract
Mitochondrial division is important for mitochondrial distribution and function. Recent data have demonstrated that ER-mitochondria contacts mark mitochondrial division sites, but the molecular basis and functions of these contacts are not understood. Here we show that in yeast, the ER-mitochondria tethering complex, ERMES, and the highly conserved Miro GTPase, Gem1, are spatially and functionally linked to ER-associated mitochondrial division. Gem1 acts as a negative regulator of ER-mitochondria contacts, an activity required for the spatial resolution and distribution of newly generated mitochondrial tips following division. Previous data have demonstrated that ERMES localizes with a subset of actively replicating mitochondrial nucleoids. We show that mitochondrial division is spatially linked to nucleoids and that a majority of these nucleoids segregate prior to division, resulting in their distribution into newly generated tips in the mitochondrial network. Thus, we postulate that ER-associated division serves to link the distribution of mitochondria and mitochondrial nucleoids in cells. DOI:http://dx.doi.org/10.7554/eLife.00422.001.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“At the fission site of mitochondria, the ERMES complex localizes adjacent to replicating mtDNA and is involved in the distribution of newly replicated mtDNA to the dividing mitochondria [33].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [33]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“After mitochondrial fission, one of the dividing mitochondria is detached from the ER, a process that requires Gem1 in S. cerevisiae [33].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [33]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In S. cerevisiae, mutations leading to decreased GTPase activity, Gem1(S19N) or Gem1(S462N), impair the maintenance of mitochondrial morphology and dissociation of ERMES from the fission site [33].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [33]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“The fission site of mitochondria is wrapped around by ER tubules [44], where the ERMES complex localizes [33].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [33]
The cited source says what the claim attributes to it.
In the citing paper
“As the ERMES plays an important role in mitochondrial fission [33], the impact of each subunit on azole resistance was evaluated.”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [33]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Computer Visualization of Three-Dimensional Image Data Using IMOD
Kremer, J. R., Mastronarde, D. N., & McIntosh, J. R. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0013 · Cited by 5,530
Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N. G., Palmer, A. E., & Tsien, R. Y. (2004) · Nature Biotechnology · doi:10.1038/nbt1037 · Cited by 4,619
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248 · cited 2×
“The detection of ERMES foci by fluorescence imaging may underestimate ERMES foci associated with mitochondrial division as we observed a positive correlation between the percentage of mitochondrial divisions associated with a given ERMES subunit and its estimated whole-cell abundance (Huh et al., 2003).”
BackgroundBrachmann, C. B., Davies, A., Cost, G. J., Caputo, E. M., Li, J., Hieter, P., & Boeke, J. D. (1998) · Yeast · doi:10.1002/(sici)1097-0061(19980130)14:2 · Cited by 3,418
[12] One-step gene disruption in yeast
Rothstein, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)01015-0 · Cited by 3,282
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Janke, C., Magiera, M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A. C., Doenges, G., Schwob, E., Schiebel, E., et al. (2004) · Yeast · doi:10.1002/yea.1142 · Cited by 2,251
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
Self-citationAn 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
Self-citationPINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,198
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 325
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
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex
Jeong, H., Park, J., & Lee, C. (2016) · EMBO Reports · doi:10.15252/embr.201642706 · Cited by 71
One ring to bring them all and in the darkness bind them: The trafficking of heme without deliverers
Chambers, I. G., Willoughby, M. M., Hamza, I., & Reddi, A. R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118881 · Cited by 77
COPI selectively drives maturation of the early Golgi
Papanikou, E., Day, K. J., Austin, J. R., & Glick, B. S. (2015) · eLife · doi:10.7554/elife.13232 · Cited by 75
Mdm10 is an ancient eukaryotic porin co-occurring with the ERMES complex
Flinner, N., Ellenrieder, L., Stiller, S. B., Becker, T., Schleiff, E., & Mirus, O. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.006 · Cited by 73
Failure is not an option – mitochondrial genome segregation in trypanosomes
Schneider, A., & Ochsenreiter, T. (2018) · Journal of Cell Science · doi:10.1242/jcs.221820 · Cited by 71
Of yeast, mice and men: MAMs come in two flavors
Herrera-Cruz, M. S., & Simmen, T. (2017) · Biology Direct · doi:10.1186/s13062-017-0174-5 · Cited by 73
Carelli, V., Maresca, A., Caporali, L., Trifunov, S., Zanna, C., & Rugolo, M. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.01.023 · Cited by 74
ER-plasma membrane junctions: Why and how do we study them?
Chang, C., Chen, Y., & Liou, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.018 · Cited by 74
Regulation of Mitochondrial Dynamics and Autophagy by the Mitochondria-Associated Membrane
Tagaya, M., & Arasaki, K. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_3 · Cited by 74
Mitochondrial lipid transport at a glance
Scharwey, M., Tatsuta, T., & Langer, T. (2013) · Journal of Cell Science · doi:10.1242/jcs.134130 · Cited by 74
An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion
Nguyen, T. T., & Voeltz, G. K. (2022) · eLife · doi:10.7554/elife.84279 · Cited by 68
Self-citationHerrera-Cruz, M. S., & Simmen, T. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_2 · Cited by 68
Tucey, T. M., Verma-Gaur, J., Nguyen, J., Hewitt, V. L., Lo, T. L., Shingu-Vazquez, M., Robertson, A. A. B., Hill, J. R., Pettolino, F. A., Beddoe, T., et al. (2016) · mSphere · doi:10.1128/msphere.00074-16 · Cited by 66
Autophagy balances mtDNA synthesis and degradation by DNA polymerase POLG during starvation
Medeiros, T., Thomas, R. L., Ghillebert, R., & Graef, M. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201801168 · Cited by 65
Mitochondria and the Brain: Bioenergetics and Beyond
Belenguer, P., Duarte, J. M. N., Schuck, P. F., & Ferreira, G. C. (2019) · Neurotoxicity Research · doi:10.1007/s12640-019-00061-7 · Cited by 69
Endoplasmic Reticulum–Mitochondria Contact Sites—Emerging Intracellular Signaling Hubs
Aoyama-Ishiwatari, S., & Hirabayashi, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653828 · Cited by 66
Miro's N-Terminal GTPase Domain Is Required for Transport of Mitochondria into Axons and Dendrites
Babić, M., Russo, G. J., Wellington, A. J., Sangston, R., Gonzalez, M., & Zinsmaier, K. E. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1035-14.2015 · Cited by 67
Laar, V. S. V., Arnold, B. A., Howlett, E. H., Calderon, M. J., Croix, C. M. S., Greenamyre, J. T., Sanders, L. H., & Berman, S. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0541-18.2018 · Cited by 65
Colpman, P., Dasgupta, A., & Archer, S. L. (2023) · Cells · doi:10.3390/cells12141897 · Cited by 66
Separating and Segregating the Human Mitochondrial Genome
Nicholls, T. J. J., & Gustafsson, C. M. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.08.007 · Cited by 65
Mitochondria-associated membranes: A hub for neurodegenerative diseases
Liu, J., & Yang, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112890 · Cited by 67
In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts
Sesaki, H., Adachi, Y., Kageyama, Y., Itoh, K., & Iijima, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.024 · Cited by 62
Koh, J., Kim, Y., Seo, D. Y., & Sohn, T. S. (2021) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2021.0138 · Cited by 61
Dynamic survey of mitochondria by ubiquitin
Escobar‐Henriques, M., & Langer, T. (2014) · EMBO Reports · doi:10.1002/embr.201338225 · Cited by 61
Genetic instability in budding and fission yeast—sources and mechanisms
Skoneczna, A., Kaniak, A., & Skoneczny, M. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv028 · Cited by 59
Reinventing an Organelle: The Reduced Mitochondrion in Parasitic Protists
Santos, H. J., Makiuchi, T., & Nozaki, T. (2018) · Trends in Parasitology · doi:10.1016/j.pt.2018.08.008 · Cited by 61
Role of membrane contact sites in protein import into mitochondria
Horvath, S. E., Rampelt, H., Oeljeklaus, S., Warscheid, B., van der Laan, M., & Pfanner, N. (2014) · Protein Science · doi:10.1002/pro.2625 · Cited by 61
Zhang, P., Konja, D., Zhang, Y., & Wang, Y. (2021) · Cells · doi:10.3390/cells10092195 · Cited by 58
From dysfunctional endoplasmic reticulum-mitochondria coupling to neurodegeneration
Erpapazoglou, Z., Mouton‐Liger, F., & Corti, O. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.03.021 · Cited by 59
Liang, T., Hang, W., Chen, J., Wu, Y., Wen, B., Xu, K., Ding, B., & Chen, J. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00563-y · Cited by 54
Clueless/CLUH regulates mitochondrial fission by promoting recruitment of Drp1 to mitochondria
Yang, H. M., Sibilla, C., Liu, R., Yun, J., Hay, B. A., Blackstone, C. D., Chan, D. C., Harvey, R. J., & Guo, M. (2022) · Nature Communications · doi:10.1038/s41467-022-29071-4 · Cited by 60
Outer membrane protein functions as integrator of protein import and DNA inheritance in mitochondria
Käser, S., Oeljeklaus, S., Týč, J., Vaughan, S., Warscheid, B., & Schneider, A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605497113 · Cited by 54
Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy
Belgareh‐Touzé, N., Cavellini, L., & Cohen, M. M. (2016) · Autophagy · doi:10.1080/15548627.2016.1252889 · Cited by 54
Mitochondrial adventures at the organelle society
Diogo, C. V., Yambire, K. F., Fernández-Mosquera, L., Fonseca, T. B., & Raimundo, N. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.04.124 · Cited by 55
Mitochondrial Fission: Regulation and ER Connection
Lee, H., & Yoon, Y. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.2329 · Cited by 53
TAC102 Is a Novel Component of the Mitochondrial Genome Segregation Machinery in Trypanosomes
Trikin, R. M., Doiron, N., Hoffmann, A., Haenni, B., Jakob, M., Schnaufer, A. C., Schimanski, B., Zuber, B., & Ochsenreiter, T. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005586 · Cited by 46
Modulation of Mitochondrial Dynamics in Neurodegenerative Diseases: An Insight Into Prion Diseases
Zhu, T., Chen, J., Wang, Q., Shao, W., & Qi, B. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00336 · Cited by 53
Mitofusins: from mitochondria to fertility
Zhao, S., Heng, N., Wang, H., Wang, H., Zhang, H., Gong, J., Hu, Z., & Zhu, H. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04386-z · Cited by 53
Hajnóczky, G., Booth, D., Csordás, G., Debattisti, V., Golenár, T., Naghdi, S., Niknejad, N., Paillard, M., Seifert, E. L., & Weaver, D. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.06.002 · Cited by 50
Wideman, J. G., & Muñoz-Gómez, S. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.01.015 · Cited by 47
Gunning, A. C., Strucinska, K., Oreja, M. M., Parrish, A., Caswell, R. C., Stals, K. L., Durigon, R., Durlacher, K., Cunningham, M., Grochowski, C. M., et al. (2020) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2020.01.007 · Cited by 50
Ergosterol reduction impairs mitochondrial DNA maintenance in S. cerevisiae
Cirigliano, A., Macone, A., Bianchi, M. M., Oliaro‐Bosso, S., Balliano, G., Negri, R., & Rinaldi, T. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.12.002 · Cited by 48
Ren, W., Ge, X., Li, M., Sun, J. L., Li, S., Gao, S., Shan, C., Gao, B., & Xi, P. (2024) · Light Science & Applications · doi:10.1038/s41377-024-01463-9 · Cited by 52
Organization and dynamics of yeast mitochondrial nucleoids
Miyakawa, I. (2017) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.93.021 · Cited by 57
ER–mitochondria contacts promote mitochondrial-derived compartment biogenesis
English, A. M., Schuler, M.-H., Xiao, T., Kornmann, B., Shaw, J. M., & Hughes, A. L. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202002144 · Cited by 48
Mitochondrial dynamics in aging and disease
Bereiter-Hahn, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00004-0 · Cited by 48
Balancing life and death: BCL‐2 family members at diverse ER–mitochondrial contact sites
Means, R. E., & Katz, S. G. (2021) · FEBS Journal · doi:10.1111/febs.16241 · Cited by 50
Mitochondrial movers and shapers: Recent insights into regulators of fission, fusion and transport
Fatima, N. U., & Ananthanarayanan, V. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.102150 · Cited by 48
Sharing the cell's bounty – organelle inheritance in yeast
Knoblach, B., & Rachubinski, R. A. (2015) · Journal of Cell Science · doi:10.1242/jcs.151423 · Cited by 47
Lipin1 deficiency causes sarcoplasmic reticulum stress and chaperone‐responsive myopathy
Rashid, T., Nemazanyy, I., Paolini, C., Tatsuta, T., Crespin, P., de Villeneuve, D., Brodesser, S., Bénit, P., Rustin, P., Baraibar, M. A., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899576 · Cited by 49
ER-Mitochondria Calcium Transfer, Organelle Contacts and Neurodegenerative Diseases
Vallese, F., Barazzuol, L., Maso, L., Brini, M., & Calí, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-12457-1_29 · Cited by 48
Martinez-Guzman, O., Willoughby, M. M., Saini, A. G., Dietz, J. V., Bohovych, I., Medlock, A. E., Khalimonchuk, O., & Reddi, A. R. (2020) · Journal of Cell Science · doi:10.1242/jcs.237917 · Cited by 47
The Emerging Role of RHOT1/Miro1 in the Pathogenesis of Parkinson's Disease
Großmann, D., Berenguer-Escuder, C., Chemla, A., Arena, G., & Krüger, R. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00587 · Cited by 55
Better to keep in touch: investigating inter‐organelle cross‐talk
Rossini, M., Pizzo, P., & Filadi, R. (2020) · FEBS Journal · doi:10.1111/febs.15451 · Cited by 49
Panchal, K., & Tiwari, A. K. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.10.005 · Cited by 49
Splitting up the powerhouse: structural insights into the mechanism of mitochondrial fission
Richter, V., Singh, A. P., Kvansakul, M., Ryan, M. T., & Osellame, L. D. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1950-y · Cited by 48
Lipid synthesis and membrane contact sites: a crossroads for cellular physiology
Fernández-Murray, J. P., & McMaster, C. R. (2016) · Journal of Lipid Research · doi:10.1194/jlr.r070920 · Cited by 45
Michalska, B., Kwapiszewska, K., Szczepanowska, J., Kalwarczyk, T., Patalas‐Krawczyk, P., Szczepański, K., Hołyst, R., Duszyński, J., & Szymański, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-26578-z · Cited by 46
Developmental regulation of an organelle tether coordinates mitochondrial remodeling in meiosis
Sawyer, E. M., Joshi, P. R., Jorgensen, V., Yunus, J., Berchowitz, L. E., & Ünal, E. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201807097 · Cited by 48
Hu, D., Liu, Z., & Qi, X. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.746873 · Cited by 44
The myriad roles of Miro in the nervous system: axonal transport of mitochondria and beyond
Lee, K., & Lu, B. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00330 · Cited by 46
Stay in touch with the endoplasmic reticulum
Sun, S., Gan, Z., Jia, M., Jiang, Q., Li, S., Wang, H., Li, W., Wang, Y., Bian, X., Zhao, Y. G., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-023-2443-9 · Cited by 45
Mitochondria-driven assembly of a cortical anchor for mitochondria and dynein
Kraft, L. M., & Lackner, L. L. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201702022 · Cited by 42
Self-citationOrtiz-Sandoval, C. G., Hughes, S. C., Dacks, J. B., & Simmen, T. (2014) · Cellular Logistics · doi:10.4161/21592799.2014.986399 · Cited by 41
Mitochondrial Dynamics: ER Actin Tightens the Drp1 Noose
Prudent, J., & McBride, H. M. (2016) · Current Biology · doi:10.1016/j.cub.2016.01.009 · Cited by 43
Sinzel, M., Tan, T., Wendling, P., Kalbacher, H., Özbalci, C., Chelius, X., Westermann, B., Brügger, B., Rapaport, D., & Dimmer, K. (2016) · EMBO Reports · doi:10.15252/embr.201541273 · Cited by 42
Integrating mitochondrial organization and dynamics with cellular architecture
Jayashankar, V., & Rafelski, S. M. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.09.002 · Cited by 42
Rasul, F., Zheng, F., Dong, F., He, J., Liu, L., Liu, W., Cheema, J. Y., Wei, W., & Fu, C. (2021) · Nature Communications · doi:10.1038/s41467-020-20866-x · Cited by 35
Morphological control of mitochondrial bioenergetics
Yoon, Y. (2015) · Frontiers in bioscience · doi:10.2741/4306 · Cited by 41
Closing the Gap: Membrane Contact Sites in the Regulation of Autophagy
Kohler, V., Aufschnaiter, A., & Büttner, S. (2020) · Cells · doi:10.3390/cells9051184 · Cited by 42
Controlling the topology of mammalian mitochondrial DNA
Menger, K. E., Rodríguez‐Luis, A., Chapman, J., & Nicholls, T. J. J. (2021) · Open Biology · doi:10.1098/rsob.210168 · Cited by 40
Jimenez, L., Laporte, D., Duvezin‐Caubet, S., Courtout, F., & Sagot, I. (2013) · Journal of Cell Science · doi:10.1242/jcs.137141 · Cited by 42
Vimar Is a Novel Regulator of Mitochondrial Fission through Miro
Ding, L., Ye, L., Han, Y., Li, Y., Ji, X., & Liu, L. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006359 · Cited by 36
GBF1 and Arf1 interact with Miro and regulate mitochondrial positioning within cells
Walch, L., Pellier, E., Leng, W., Lakisic, G., Gautreau, A. M., Contremoulins, V., Verbavatz, J., & Jackson, C. L. (2018) · Scientific Reports · doi:10.1038/s41598-018-35190-0 · Cited by 37
Mind the Gap: Mitochondria and the Endoplasmic Reticulum in Neurodegenerative Diseases
Leal, N. S., & Martins, L. M. (2021) · Biomedicines · doi:10.3390/biomedicines9020227 · Cited by 40
Chemical inhibition of mitochondrial fission via targeting the DRP1-receptor interaction
Yang, J., Chen, P., Cao, Y., Liu, S., Wang, W., Li, L., Li, J., Jiang, Z., Ma, Y., Chen, S., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.002 · Cited by 36
LonP1 Links Mitochondria–ER Interaction to Regulate Heart Function
Li, Y., Huang, D., Jia, L., Shangguan, F., Gong, S., Lan, L., Song, Z., Xu, J., Yan, C., Chen, T., et al. (2023) · Research · doi:10.34133/research.0175 · Cited by 39
Hönscher, C., & Ungermann, C. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.875512 · Cited by 36
Reactive oxygen species triggers unconventional secretion of antioxidants and Acb1
Cruz-García, D., Brouwers, N., Malhotra, V., & Curwin, A. J. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201905028 · Cited by 36
The multifunctional nature of mitochondrial contact site proteins
Harper, C. S., White, A. J., & Lackner, L. L. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.02.010 · Cited by 35
Self-citationMitochondrial dynamics in parasitic protists
Voleman, L., & Doležal, P. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008008 · Cited by 34
Connection of Protein Transport and Organelle Contact Sites in Mitochondria
Ellenrieder, L., Rampelt, H., & Becker, T. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.023 · Cited by 33
Voleman, L., Najdrová, V., Ástvaldsson, Á., Tůmová, P., Einarsson, E., Švindrych, Z., Hagen, G. M., Tachezy, J., Svärd, S. G., & Doležal, P. (2017) · BMC Biology · doi:10.1186/s12915-017-0361-y · Cited by 33
Egea, P. F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.784367 · Cited by 35
Mitochondria-associated endoplasmic reticulum membranes in the heart
Wu, S., & Zou, M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.018 · Cited by 33
The endoplasmic reticulum-the caring mother of the cell
Spang, A. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.06.004 · Cited by 31
Mitochondrial Dynamics and Heart Failure
Knowlton, A. A., & Liu, T. (2015) · Comprehensive physiology · doi:10.1002/cphy.c150022 · Cited by 32
Mitochondrial Structure, Dynamics, and Physiology: Light Microscopy to Disentangle the Network
Landoni, J. C., Kleele, T., Winter, J., Stepp, W. L., & Manley, S. (2024) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111822-114733 · Cited by 32
The ERMES (Endoplasmic Reticulum and Mitochondria Encounter Structures) mediated functions in fungi
Kundu, D., & Pasrija, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.02.010 · Cited by 29
VPS13D interacts with VCP/p97 and negatively regulates ER- mitochondrial interactions
Du, Y., Wang, J., Xiong, J., Fang, N., & Ji, W.-K. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-03-0097 · Cited by 30
ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria
Koch, C., Schuldiner, M., & Herrmann, J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179655 · Cited by 30
The mitochondrial Ras-related GTPase Miro: views from inside and outside the metazoan kingdom
Yamaoka, S., & Hara‐Nishimura, I. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00350 · Cited by 30
Dynamic Regulation of Peroxisomes and Mitochondria during Fungal Development
Navarro-Espíndola, R., Suaste-Olmos, F., & Peraza‐Reyes, L. (2020) · Journal of Fungi · doi:10.3390/jof6040302 · Cited by 30
The Role of PTEN-L in Modulating PINK1-Parkin-Mediated Mitophagy
Eldeeb, M. A., Esmaili, M., Hassan, M., & Ragheb, M. A. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00475-w · Cited by 30
Bridging lipid metabolism and mitochondrial genome maintenance
Boone, C., & Lewis, S. C. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107498 · Cited by 27
Quiescent cell re-entry is limited by macroautophagy-induced lysosomal damage
Murley, A., Popovici, A. C., Hu, X., Lund, A., Wickham, K., Durieux, J., Joe, L. K., Koronyo, E., Zhang, H., Genuth, N. R., et al. (2025) · Cell · doi:10.1016/j.cell.2025.03.009 · Cited by 31
Self-citationMitochondrial-derived vesicles in skeletal muscle remodeling and adaptation
Picca, A., Guerra, F., Calvani, R., Romanò, R., Coelho‐Júnior, H. J., Bucci, C., Leeuwenburgh, C., & Marzetti, E. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.023 · Cited by 28
Interaction of MDM33 with mitochondrial inner membrane homeostasis pathways in yeast
Klecker, T., Wemmer, M., Haag, M., Weig, A. R., Böckler, S., Langer, T., Nunnari, J. M., & Westermann, B. (2015) · Scientific Reports · doi:10.1038/srep18344 · Cited by 26
Self-citationInsight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase
Smith, K. P., Focia, P. J., Chakravarthy, S., Landahl, E. C., Klosowiak, J. L., Rice, S. E., & Freymann, D. M. (2019) · Journal of Structural Biology · doi:10.1016/j.jsb.2020.107656 · Cited by 29
Metadata
- Authors
- Murley, A., Lackner, L. L., Osman, C., West, M., Voeltz, G. K., Walter, P., & Nunnari, J.
- Affiliations
- University of California, Davis (US)
- University of California, San Francisco (US)
- University of Colorado Boulder (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nunnari, Jodi
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2013-05-14
- Volume
- 2
- Pages
- e00422-e00422
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC3654481
- OpenAlex
- W2130893307
- Cited by
- 326
- References
- 55
- Citations by year
- 2026: 7 · 2025: 20 · 2024: 17 · 2023: 16 · 2022: 19 · 2021: 26 · 2020: 34 · 2019: 27 · 2018: 32 · 2017: 26 · 2016: 29 · 2015: 28 · 2014: 31 · 2013: 14
- FWCI
- 15.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institutes of Health (5T32GM007377-34, R01GM097432, RO1GM083977)
- Howard Hughes Medical Institute
- Human Frontier Science Program
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- mitochondrial division, ER-mitochondria contact sites, ERMES, mitochondrial nucleoids, mitochondrial DNA segregation, mitochondrial distribution, yeast
- MeSH terms
- DNA, Fungal, DNA, Mitochondrial, Endoplasmic Reticulum, Mitochondria, Saccharomyces cerevisiae, Signal Transduction, Saccharomyces cerevisiae Proteins, Multiprotein Complexes, Mitochondrial Dynamics
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
