The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
The Scaffold Protein Atg11 Recruits Fission Machinery to Drive Selective Mitochondria Degradation by Autophagy
Open accessAbstract
SUMMARY As the cellular power plant, mitochondria play a significant role in homeostasis. To maintain the proper quality and quantity of mitochondria requires both mitochondrial degradation and division. A selective type of autophagy, mitophagy, drives the degradation of excess or damaged mitochondria, whereas division is controlled by a specific fission complex; however, the relationship between these two processes, especially the role of mitochondrial fission during mitophagy, remains unclear. In this study, we report that mitochondrial fission is important for the progression of mitophagy When mitophagy is induced, the fission complex is recruited to the degrading mitochondria through an interaction between Atg11 and Dnm1; interfering with this interaction severely blocks mitophagy. These data establish a paradigm for selective organelle degradation.
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.
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
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
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · cited 1×
“Work inmammalian cells suggests that mitochondrial fission facilitates the process of mitophagy (Tanaka et al., 2010; Twig et al., 2008); however, it is not clear whether these two processes occur independently or whether they function in a coordinated manner.”
BackgroundPINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944
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
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616
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 · cited 1×
“Work inmammalian cells suggests that mitochondrial fission facilitates the process of mitophagy (Tanaka et al., 2010; Twig et al., 2008); however, it is not clear whether these two processes occur independently or whether they function in a coordinated manner.”
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
Mechanism of Cargo Selection in the Cytoplasm to Vacuole Targeting Pathway
Shintani, T., Huang, W.-P., Stromhaug, P. E., & Klionsky, D. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00373-8 · Cited by 362
Self-citationMitophagy in Yeast Occurs through a Selective Mechanism
Kanki, T., & Klionsky, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802403200 · Cited by 335
Self-citationPpAtg30 Tags Peroxisomes for Turnover by Selective Autophagy
Farré, J.-C., Manjithaya, R., Mathewson, R. D., & Subramani, S. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.12.011 · Cited by 331
Research works printed but not linked: 30
- Aoki, 2011, Phosphorylation of Serine 114 on Atg32 mediates mitophagy, Mol. Biol. Cell, 22, 3206, 10.1091/mbc.e11-02-0145 · DOI · Paper page
- Baba, 1997, Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome, J. Cell Biol., 139, 1687, 10.1083/jcb.139.7.1687 · DOI · Paper page
- Bleazard, 1999, The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast, Nat. Cell Biol., 1, 298, 10.1038/13014 · DOI · Paper page
- Friedman, 2011, ER tubules mark sites of mitochondrial division, Science, 334, 358, 10.1126/science.1207385 · DOI · Paper page
- Fukushima, 2001, The GTPase effector domain sequence of the Dnm1p GTPase regulates self-assembly and controls a rate-limiting step in mitochondrial fission, Mol. Biol. Cell, 12, 2756, 10.1091/mbc.12.9.2756 · DOI
- Griffin, 2005, The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria, J. Cell Biol., 170, 237, 10.1083/jcb.200503148 · DOI · Paper page
- Hutchins, 1999, Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway, J. Cell Sci., 112, 4079, 10.1242/jcs.112.22.4079 · DOI · Paper page
- Kanki, 2009, Mitochondrial abnormalities drive cell death in Wolfram syndrome 2, Cell Res., 19, 922, 10.1038/cr.2009.94 · doi:10.1038/cr.2009.94
- Kanki, 2009, A genomic screen for yeast mutants defective in selective mitochondria autophagy, Mol. Biol. Cell, 20, 4730, 10.1091/mbc.e09-03-0225 · DOI · Paper page
- Kanki, 2009, Atg32 is a mitochondrial protein that confers selectivity during mitophagy, Dev. Cell, 17, 98, 10.1016/j.devcel.2009.06.014 · DOI · Paper page
- Karren, 2005, The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly, J. Cell Biol., 171, 291, 10.1083/jcb.200506158 · DOI
- Kim, 2001, Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole, J. Cell Biol., 153, 381, 10.1083/jcb.153.2.381 · DOI · Paper page
- Kondo-Okamoto, 2012, Autophagy-related protein 32 acts as autophagic degron and directly initiates mitophagy, J. Biol. Chem., 287, 10631, 10.1074/jbc.M111.299917 · DOI
- Kuravi, 2006, Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance in Saccharomyces cerevisiae, J. Cell Sci., 119, 3994, 10.1242/jcs.03166 · DOI · Paper page
- Mao, 2011, Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae, J. Cell Biol., 193, 755, 10.1083/jcb.201102092 · DOI · Paper page
- Mendl, 2011, Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2, J. Cell Sci., 124, 1339, 10.1242/jcs.076406 · DOI · Paper page
- Mijaljica, 2012, Receptor protein complexes are in control of autophagy, Autophagy, 8, 1701, 10.4161/auto.21332 · DOI
- Motley, 2008, Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p, J. Cell Sci., 121, 1633, 10.1242/jcs.026344 · DOI
- Motley, 2012, Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae, EMBO J., 31, 2852, 10.1038/emboj.2012.151 · DOI · Paper page
- Mozdy, 2000, Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p, J. Cell Biol., 151, 367, 10.1083/jcb.151.2.367 · DOI · Paper page
- Naylor, 2006, Mdv1 interacts with assembled dnm1 to promote mitochondrial division, J. Biol. Chem., 281, 2177, 10.1074/jbc.M507943200 · DOI
- Okamoto, 2005, Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes, Annu. Rev. Genet., 39, 503, 10.1146/annurev.genet.38.072902.093019 · DOI · Paper page
- Okamoto, 2009, Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy, Dev. Cell, 17, 87, 10.1016/j.devcel.2009.06.013 · DOI · Paper page
- Schweers, 2007, NIX is required for programmed mitochondrial clearance during reticulocyte maturation, Proc. Natl. Acad. Sci. USA, 104, 19500, 10.1073/pnas.0708818104 · DOI · Paper page
- Sung, 2007, Bimolecular fluorescence complementation analysis system for in vivo detection of protein-protein interaction in Saccharomyces cerevisiae, Yeast, 24, 767, 10.1002/yea.1504 · DOI · Paper page
- Tieu, 2000, Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division, J. Cell Biol., 151, 353, 10.1083/jcb.151.2.353 · DOI · Paper page
- Wada, 2009, Autophagy plays a role in chloroplast degradation during senescence in individually darkened leaves, Plant Physiol., 149, 885, 10.1104/pp.108.130013 · DOI · Paper page
- Xie, 2007, Autophagosome formation: core machinery and adaptations, Nat. Cell Biol., 9, 1102, 10.1038/ncb1007-1102 · DOI · Paper page
- Xie, 2008, Atg8 controls phagophore expansion during autophagosome formation, Mol. Biol. Cell, 19, 3290, 10.1091/mbc.e07-12-1292 · DOI · Paper page
- Zhang, 2010, The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B also mediates peroxisome division, Plant Cell, 22, 431, 10.1105/tpc.109.071324 · DOI
Cited by
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citationThe Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081
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
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
Self-citationRegulation of endoplasmic reticulum turnover by selective autophagy
Khaminets, A., Heinrich, T., Mari, M., Grumati, P., Huebner, A. K., Akutsu, M., Liebmann, L., Stolz, A., Nietzsche, S., Koch, N., et al. (2015) · Nature · doi:10.1038/nature14498 · Cited by 956
Murakawa, T., Yamaguchi, O., Hashimoto, A., Hikoso, S., Takeda, T., Oka, T., Yasui, H., Ueda, H., Akazawa, Y., Nakayama, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms8527 · Cited by 517
Quality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 445
Receptor-mediated mitophagy in yeast and mammalian systems
Liu, L., Sakakibara, K., Chen, Q., & Okamoto, K. (2014) · Cell Research · doi:10.1038/cr.2014.75 · Cited by 421
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363
Mitophagy: An Emerging Role in Aging and Age-Associated Diseases
Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359
Rojansky, R., Cha, M.-Y., & Chan, D. C. (2016) · eLife · doi:10.7554/elife.17896 · Cited by 336
Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2017) · Circulation · doi:10.1161/circulationaha.117.030235 · Cited by 320
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
Potential function for the Huntingtin protein as a scaffold for selective autophagy
Ochaba, J., Lukacsovich, T., Csikos, G., Zheng, S., Margulis, J., Salazar, L., Mao, K., Lau, A. L., Yeung, S. Y., Humbert, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420103111 · Cited by 308
Self-citationKIF1A/UNC-104 Transports ATG-9 to Regulate Neurodevelopment and Autophagy at Synapses
Stavoe, A. K. H., Kargbo-Hill, S. E., Hall, D. H., & Colón-Ramos, D. A. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.06.012 · Cited by 211
Anding, A. L., Wang, C., Chang, T.-K., Sliter, D. A., Powers, C. M., Hofmann, K., Youle, R. J., & Baehrecke, E. H. (2018) · Current Biology · doi:10.1016/j.cub.2017.11.064 · Cited by 172
Aparicio, R., Rana, A., & Walker, D. W. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.070 · Cited by 129
KCTD: A new gene family involved in neurodevelopmental and neuropsychiatric disorders
Teng, X., Aouacheria, A., Lionnard, L., Metz, K. A., Soane, L., Kamiya, A., & Hardwick, J. M. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13156 · Cited by 124
Abeliovich, H., Zarei, M., Rigbolt, K. T. G., Youle, R. J., & Dengjel, J. (2013) · Nature Communications · doi:10.1038/ncomms3789 · Cited by 114
Metadata
- Authors
- Mao, K., Wang, K., Liu, X., & Klionsky, D. J.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 26
- Issue
- 1
- Pages
- 9-18
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W2123779312
- Cited by
- 249
- References
- 12
- FWCI
- 19.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 379 d)
- Funders
- National Institutes of Health (GM053396)
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.