Constriction of the mitochondrial inner compartment is a priming event for mitochondrial division
Open accessAbstract
Mitochondrial division is critical for the maintenance and regulation of mitochondrial function, quality and distribution. This process is controlled by cytosolic actin-based constriction machinery and dynamin-related protein 1 (Drp1) on mitochondrial outer membrane (OMM). Although mitochondrial physiology, including oxidative phosphorylation, is also important for efficient mitochondrial division, morphological alterations of the mitochondrial inner-membrane (IMM) have not been clearly elucidated. Here we report spontaneous and repetitive constriction of mitochondrial inner compartment (CoMIC) associated with subsequent division in neurons. Although CoMIC is potentiated by inhibition of Drp1 and occurs at the potential division spots contacting the endoplasmic reticulum, it appears on IMM independently of OMM. Intra-mitochondrial influx of Ca 2+ induces and potentiates CoMIC, and leads to K + -mediated mitochondrial bulging and depolarization. Synergistically, optic atrophy 1 (Opa1) also regulates CoMIC via controlling Mic60-mediated OMM–IMM tethering. Therefore, we propose that CoMIC is a priming event for efficient mitochondrial division.
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?
The mechanism driving IMM constriction is not elucidated, but the requirement of MCU and OMA1-induced OPA1S has been shown.
“The mechanism which drives IMM constriction are not elucidated, but the requirement of MCU and OMA1-induced OPA1S has been shown [102, 103].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [102]
Inner membrane constriction occurs at ER-mitochondria contact sites before DRP1 recruitment and is independent of DRP1 action and OMM division.
“The inner membrane constriction occurs at ER–mitochondria contact sites before DRP1 recruitment and is thus independent of DRP1 action and OMM division [102, 103].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [102]
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
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575 · 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
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 · see citing works
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 · see citing works
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 · see citing works
Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
Dephosphorylation 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 · see citing works
Ishihara, 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 · see citing works
Mitochondrial fragmentation in neurodegeneration.
Knott, A. B., Perkins, G., Schwarzenbacher, R., & Bossy-Wetzel, E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2417 · Cited by 1,002 · see citing works
Dynamin, a membrane-remodelling GTPase
Ferguson, S. M., & Camilli, P. V. D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3266 · Cited by 977 · see citing works
Mitochondria and neuronal activity
Kann, O., & Kovács, R. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00222.2006 · Cited by 847 · see citing works
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 · see citing works
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817 · see citing works
The <i>i</i> -AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Anand, R., Wai, T., Baker, M. J., Kladt, N., Schauss, A. C., Rugarli, E., & Langer, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201308006 · Cited by 812 · see citing works
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 767 · see citing works
ER-mitochondria contacts couple mtDNA synthesis with mitochondrial division in human cells
Lewis, S. C., Uchiyama, L. F., & Nunnari, J. (2016) · Science · doi:10.1126/science.aaf5549 · Cited by 673 · see citing works
C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670 · see citing works
The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
Wakabayashi, J., Zhang, Z., Wakabayashi, N., Tamura, Y., Fukaya, M., Kensler, T. W., Iijima, M., & Sesaki, H. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903065 · Cited by 667 · see citing works
Self-citationDnm1 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
Mitofusin 2 ablation increases endoplasmic reticulum–mitochondria coupling
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504880112 · Cited by 578 · see citing works
Bidirectional Ca <sup>2+</sup> -dependent control of mitochondrial dynamics by the Miro GTPase
Saotome, M., Safiulina, D., Szabadkai, G., Das, S., Fransson, Å., Aspenstrom, P., Rizzuto, R., & Hajnóczky, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808953105 · Cited by 538 · see citing works
Breckenridge, D. G., Stojanovic, M., Marcellus, R. C., & Shore, G. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212059 · Cited by 533 · see citing works
Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515 · see citing works
Multiple dynamin family members collaborate to drive mitochondrial division
Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512 · see citing works
Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
Rizzuto, R., Brini, M., Pizzo, P., Murgia, M., & Pozzan, T. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00128-x · Cited by 499 · see citing works
Imaging intraorganellar Ca2+ at subcellular resolution using CEPIA
Suzuki, J., Kanemaru, K., Ishii, K., Ohkura, M., Okubo, Y., & Iino, M. (2014) · Nature Communications · doi:10.1038/ncomms5153 · Cited by 483 · see citing works
Cytoprotective Role of Ca 2+ - Activated K + Channels in the Cardiac Inner Mitochondrial Membrane
Xu, W., Liu, Y., Wang, S., McDonald, T. G., Eyk, J. E. V., Sidor, A., & O'Rourke, B. P. (2002) · Science · doi:10.1126/science.1074360 · Cited by 478 · see citing works
Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473 · see citing works
Griparić, L., van der Wel, N. N., Orozco, I. J., Peters, P. J., & van der Bliek, A. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400920200 · Cited by 468 · see citing works
CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology
Han, X.-J., Lü, Y.-F., Li, S.-A., Kaitsuka, T., Sato, Y., Tomizawa, K., Nairn, A. C., Takei, K., Matsui, H., & Matsushita, M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802164 · Cited by 423 · see citing works
Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission
Mears, J. A., Lackner, L. L., Fang, S., Ingerman, E., Nunnari, J. M., & Hinshaw, J. E. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1949 · Cited by 418 · see citing works
Composition and dynamics of human mitochondrial nucleoids.
Garrido, N., Griparić, L., Jokitalo, E., Wartiovaara, J., van der Bliek, A. M., & Spelbrink, J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0399 · Cited by 390 · see citing works
Logan, C. V., Szabadkai, G., Sharpe, J. A., Parry, D. A., Torelli, S., Childs, A., Kriek, M., Phadke, R., Johnson, C. A., Roberts, N. Y., et al. (2013) · Nature Genetics · doi:10.1038/ng.2851 · Cited by 369 · see citing works
Germain, M., Mathai, J. P., McBride, H. M., & Shore, G. C. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600592 · Cited by 337 · see citing works
Darshi, M., Mendiola, V. L., Mackey, M. R., Murphy, A. N., Koller, A. A., Perkins, G. A., Ellisman, M. H., & Taylor, S. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171975 · Cited by 325 · see citing works
Liu, X., & Hajnóczky, G. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.13 · Cited by 285 · see citing works
Mammalian Dynamin-like Protein DLP1 Tubulates Membranes
Yoon, Y., Pitts, K. R., & McNiven, M. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2894 · Cited by 285 · see citing works
Regulation of mitochondrial matrix volume
Kaasik, A., Safiulina, D., Zharkovsky, A., & Veksler, V. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00272.2006 · Cited by 259 · see citing works
Altered brain energetics induces mitochondrial fission arrest in Alzheimer’s Disease
Zhang, L., Trushin, S., Christensen, T. A., Bachmeier, B. V., Gateno, B., Schroeder, A., Yao, J., Itoh, K., Sesaki, H., Poon, W. W., et al. (2016) · Scientific Reports · doi:10.1038/srep18725 · Cited by 198 · see citing works
Self-citationConstriction and Dnm1p Recruitment Are Distinct Processes in Mitochondrial Fission
Legesse-Miller, A., Massol, R., & Kirchhausen, T. L. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-10-0657 · Cited by 197 · see citing works
Dickey, A. S., & Strack, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3159-11.2011 · Cited by 197 · see citing works
Mitochondrial potassium channels
Szewczyk, A. M., Jarmuszkiewicz, W., & Kunz, W. S. (2009) · IUBMB Life · doi:10.1002/iub.155 · Cited by 181 · see citing works
Breckwoldt, M. O., Pfister, F., Bradley, P. M., Marinković, P., Williams, P. R., Brill, M. S., Plomer, B., Schmalz, A., Clair, D. K. S., Naumann, R., et al. (2014) · Nature Medicine · doi:10.1038/nm.3520 · Cited by 178 · see citing works
Xu, S., Pi, H., Chen, Y., Zhang, N., Guo, P., Lu, Y., He, M., Xie, J., Zhong, M., Zhang, Y., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.7 · Cited by 160 · see citing works
Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga
Nishida, K., Takahara, M., Miyagishima, S.-Y., Kuroiwa, H., Matsuzaki, M., & Kuroiwa, T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0436886100 · Cited by 154 · see citing works
Chang, K. T., Niescier, R. F., & Min, K.-T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106862108 · Cited by 153 · see citing works
Thread-grain transition of mitochondrial reticulum as a step of mitoptosis and apoptosis
Skulachev, V. P., Bakeeva, L. E., Chernyak, B. V., Domnina, L. V., Minin, A. А., Pletjushkina, O. Y., Saprunova, V. B., Skulachev, I. V., Tsyplenkova, V. G., Vasiliev, J. M., et al. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009880.94044.49 · Cited by 150 · see citing works
Mechanical stimulation induces formin-dependent assembly of a perinuclear actin rim
Shao, X., Li, Q., Mogilner, A., Bershadsky, A. D., & Shivashankar, G. V. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504837112 · Cited by 144 · see citing works
Hom, J., Gewandter, J. S., Michael, L., Sheu, S., & Yoon, Y. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21051 · Cited by 142 · see citing works
Tamai, S., Iida, H., Yokota, S., Sayano, T., Kiguchiya, S., Ishihara, N., Hayashi, J.-I., Mihara, K., & Oka, T. (2008) · Journal of Cell Science · doi:10.1242/jcs.026625 · Cited by 134 · see citing works
Mitofilin and CHCHD6 physically interact with Sam50 to sustain cristae structure
Ding, C.-L., Wu, Z., Huang, L. H., Wang, Y., Xue, J., Chen, S., Deng, Z., Wang, L., Song, Z., & Chen, S. (2015) · Scientific Reports · doi:10.1038/srep16064 · Cited by 133 · see citing works
Atypical mitochondrial fission upon bacterial infection
Stavru, F., Palmer, A. E., Wang, C., Youle, R. J., & Cossart, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315784110 · Cited by 129 · see citing works
Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes
Hom, J., Yu, T., Yoon, Y., Porter, G. A., Jr., & Sheu, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.018 · Cited by 128 · see citing works
A Bcl-xL–Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis
Li, H., Alavian, K. N., Lazrove, E., Mehta, N., Jones, A., Zhang, P., Licznerski, P., Graham, M. M., Uo, T., Guo, J., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2791 · Cited by 123 · see citing works
Elde, N. C., Morgan, G., Winey, M., Sperling, L., & Turkewitz, A. P. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010052 · Cited by 107 · see citing works
MacVicar, T., & Lane, J. D. (2014) · Journal of Cell Science · doi:10.1242/jcs.144337 · Cited by 102 · see citing works
OPA1 promotes pH flashes that spread between contiguous mitochondria without matrix protein exchange
Domingo, J. S., Giacomello, M., Poburko, D., Scorrano, L., & Demaurex, N. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.124 · Cited by 100 · see citing works
Mitochondrial pleomorphy in plant cells is driven by contiguous ER dynamics
Jaipargas, E.-A., Barton, K. A., Mathur, N., & Mathur, J. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00783 · Cited by 97 · see citing works
OPA1 functionally interacts with MIC60 but is dispensable for crista junction formation
Barrera, M., Koob, S., Dikov, D., Vogel, F., & Reichert, A. S. (2016) · FEBS Letters · doi:10.1002/1873-3468.12384 · Cited by 94 · see citing works
Rajala, N. K. M., Gerhold, J. M., Martinsson, P., Klymov, A., & Spelbrink, J. N. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt988 · Cited by 87 · see citing works
CDK5-dependent inhibitory phosphorylation of Drp1 during neuronal maturation
Cho, B., Cho, H. M., Kim, H. J., Jeong, J., Park, S. K., Hwang, E. M., Park, J., Kim, W. R., Kim, H., & Sun, W. (2014) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.36 · Cited by 84 · see citing works
Self-citationGlutamate-induced Assembly of Bacterial Cell Division Protein FtsZ
Beuria, T. K., Krishnakumar, S. S., Sahar, S., Singh, N., Gupta, K. K., Meshram, M., & Panda, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205760200 · Cited by 67 · see citing works
Delayed neuronal preconditioning by NS1619 is independent of calcium activated potassium channels
Gáspár, T., Katakam, P. V. G., Snipes, J. A., Kis, B., Domoki, F., Bari, F., & Busija, D. W. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05210.x · Cited by 62 · see citing works
The Effect of OPA1 on Mitochondrial Ca2+ Signaling
Fülöp, L., Szanda, G., Enyedi, B., Várnai, P., & Spät, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025199 · Cited by 60 · see citing works
Brustovetsky, T., Li, V., & Brustovetsky, N. (2009) · Cell Calcium · doi:10.1016/j.ceca.2009.03.017 · Cited by 52 · see citing works
Lee, H., & Yoon, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.533299 · Cited by 51 · see citing works
Mitochondrial Division in Rat Cardiomyocytes: An Electron Microscope Study
Fujioka, H., Tandler, B., & Hoppel, C. L. (2012) · The Anatomical Record · doi:10.1002/ar.22523 · Cited by 51 · see citing works
Kuroiwa, T., Misumi, O., Nishida, K., Yagisawa, F., Yoshida, Y., Fujiwara, T., & Kuroiwa, H. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01203-3 · Cited by 44 · see citing works
Aquaporin-assisted and ER-mediated mitochondrial fission: A hypothesis
Lee, J.-S., Hou, X., Bishop, N. M., Wang, S., Flack, A., Cho, W. J., Chen, X., Mao, G., Taatjes, D. J., Sun, F., et al. (2013) · Micron · doi:10.1016/j.micron.2013.01.005 · Cited by 19 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Chakrabarti, R., Ji, W.-K., Stan, R. V., de Juan Sanz, J., Ryan, T. A., & Higgs, H. N. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709111 · Cited by 349 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
- Authors
- Cho, B., Cho, H. M., Jo, Y., Kim, H. D., Song, M., Moon, C., Kim, H., Kim, K., Sesaki, H., Rhyu, I. J., Kim, H., & Sun, W.
- Affiliations
- Daegu Gyeongbuk Institute of Science and Technology (KR)
- Korea University (KR)
- Seoul National University (KR)
- Yonsei University (KR)
- Johns Hopkins University (US)
- Corresponding author
- Sun, Woong
- ORCID
- Venue
- Nature Communications
- Published
- 2017-06-09
- Volume
- 8
- Issue
- 1
- Pages
- 15754-15754
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC5472732
- OpenAlex
- W2621744935
- Cited by
- 179
- References
- 71
- Citations by year
- 2026: 13 · 2025: 20 · 2024: 12 · 2023: 23 · 2022: 21 · 2021: 29 · 2020: 20 · 2019: 17 · 2018: 20 · 2017: 4
- FWCI
- 6.81
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by-nc-nd)
- Funders
- National Research Foundation (2015M3C7A1028790, NRF-2015M3C7A1028790)
- Ulsan National Institute of Science and Technology
- Ewha Womans University
- Daegu Gyeongbuk Institute of Science and Technology
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM089853)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondrial division, Drp1, mitochondrial outer membrane, endoplasmic reticulum, calcium influx, mitochondrial depolarization, OPA1, Mic60, mitochondrial fusion, neurons
- MeSH terms
- Animals, Calcium, Humans, Microtubule-Associated Proteins, Mitochondria, Neurons, Rats, Sprague-Dawley, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins, Mitochondrial Membranes, Rats, 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
