Ceramide targets autophagosomes to mitochondria and induces lethal mitophagy
Open accessAbstract
Mechanisms by which autophagy promotes cell survival or death are unclear. We provide evidence that C(18)-pyridinium ceramide treatment or endogenous C(18)-ceramide generation by ceramide synthase 1 (CerS1) expression mediates autophagic cell death, independent of apoptosis in human cancer cells. C(18)-ceramide-induced lethal autophagy was regulated via microtubule-associated protein 1 light chain 3 β-lipidation, forming LC3B-II, and selective targeting of mitochondria by LC3B-II-containing autophagolysosomes (mitophagy) through direct interaction between ceramide and LC3B-II upon Drp1-dependent mitochondrial fission, leading to inhibition of mitochondrial function and oxygen consumption. Accordingly, expression of mutant LC3B with impaired ceramide binding, as predicted by molecular modeling, prevented CerS1-mediated mitochondrial targeting, recovering oxygen consumption. Moreover, knockdown of CerS1 abrogated sodium selenite-induced mitophagy, and stable LC3B knockdown protected against CerS1- and C(18)-ceramide-dependent mitophagy and blocked tumor suppression in vivo. Thus, these data suggest a new receptor function of ceramide for anchoring LC3B-II autophagolysosomes to mitochondrial membranes, defining a key mechanism for the induction of lethal mitophagy.
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Localization of CerS1 to the mitochondria and synthesis of ceramide in the outer mitochondrial membrane recruit the autophagic machinery and induce mitophagy by binding autophagosome-associated LC3.
“The localization of CerS1 to the mitochondria and the synthesis of ceramide in the outer mitochondrial membrane recruit the autophagic machinery and induce mitophagy (15) by binding autophagosome-associated LC3.”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [15]
The Results sections on CerS1/C18-ceramide–LC3B-II interaction and mitochondrial mitophagy report CerS1-induced ceramide on the mitochondrial outer membrane and indicate that ceramide–LC3B interaction targets autophagic structures to mitochondria. The passages establish localization of the ceramide, not localization of CerS1 itself or the site where ceramide is synthesized; those parts of the claim are unsupported. (LLM, conf=0.86)
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1 retracted
Huang, Q. B., Wu, Y., Tan, H.-L., Ong, C.-N., & Shen, H.-M. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.151 · Cited by 111 · see citing works
RetractedAutophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,467 · see citing works
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452 · 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
Eaten alive: a history of macroautophagy
Yang, Z., & Klionsky, D. J. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-814 · Cited by 2,096 · see citing works
Rabinowitz, J. D., & White, E. (2010) · Science · doi:10.1126/science.1193497 · Cited by 1,982 · see citing works
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555 · see citing works
Lindsten, T., Ross, A. J., King, A., Zong, W.-X., Rathmell, J. C., Shiels, H. A., Ulrich, E., Waymire, K. G., Mahar, P., Frauwirth, K., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00136-2 · Cited by 1,489 · see citing works
Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
Shimizu, S., Kanaseki, T., Mizushima, N., Mizuta, T., Arakawa-Kobayashi, S., Thompson, C. B., & Tsujimoto, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1192 · Cited by 1,358 · see citing works
Biologically active sphingolipids in cancer pathogenesis and treatment
Öğretmen, B., & Hannun, Y. A. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1411 · Cited by 1,216 · see citing works
Molecular machinery for non-vesicular trafficking of ceramide
Hanada, K., Kumagai, K., Yasuda, S., Miura, Y., Kawano‐Kawada, M., Fukasawa, M., & Nishijima, M. (2003) · Nature · doi:10.1038/nature02188 · Cited by 1,051 · see citing works
Salazar‐Roa, M., Carracedo, A., Salanueva, Í. J., Hernández‐Tiedra, S., Lorente, M., Egia, A., Vázquez, P., Blázquez, C., Torres, S., Garcia, S., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37948 · Cited by 686 · see citing works
Scarlatti, F., Bauvy, C., Ventruti, A., Sala, G., Cluzeaud, F., Vandewalle, A., Ghidoni, R., & Codogno, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313561200 · Cited by 451 · see citing works
Kinase Suppressor of Ras Is Ceramide-Activated Protein Kinase
Zhang, Y., Yao, B., Delikat, S. E., Bayoumy, S. S., Lin, X., Basu, S., McGinley, M., Chan-Hui, P.-Y., Lichenstein, H. S., & Kolesnick, R. (1997) · Cell · doi:10.1016/s0092-8674(00)80183-x · Cited by 437 · see citing works
When Do Lasses (Longevity Assurance Genes) Become CerS (Ceramide Synthases)?
Pewzner-Jung, Y., Ben-Dor, S., & Futerman, A. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600010200 · Cited by 435 · see citing works
Satoo, K., Noda, N. N., Kumeta, H., Fujioka, Y., Mizushima, N., Ohsumi, Y., & Inagaki, F. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.80 · Cited by 381 · see citing works
Tracker Dyes to Probe Mitochondrial Autophagy (Mitophagy) in Rat Hepatocytes
Rodríguez‐Enríquez, S., Kim, I., Currin, R. T., & Lemasters, J. J. (2006) · Autophagy · doi:10.4161/auto.2229 · Cited by 331 · see citing works
Self-citationVenkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J. C., Sullards, M. C., Merrill, A. H., & Futerman, A. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205211200 · Cited by 282 · see citing works
Bnip3 impairs mitochondrial bioenergetics and stimulates mitochondrial turnover
Rikka, S., Quinsay, M. N., Thomas, R. L., Kubli, D. A., Zhang, X., Murphy, A. N., & Gustafsson, Å. B. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.146 · Cited by 277 · see citing works
Vara‐Ciruelos, D., Salazar‐Roa, M., Olea‐Herrero, N., Guzmán, M., Velasco, G., & Díaz‐Laviada, I. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.32 · Cited by 268 · see citing works
Lavieu, G., Scarlatti, F., Sala, G., Carpentier, S., Levade, T., Ghidoni, R., Botti, J., & Codogno, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m506182200 · Cited by 257 · see citing works
Senkal, C. E., Ponnusamy, S., Bielawski, J., Hannun, Y. A., & Öğretmen, B. (2009) · The FASEB Journal · doi:10.1096/fj.09-135087 · Cited by 254 · see citing works
Self-citationTanida, I., Ueno, T., & Kominami, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407016200 · Cited by 244 · see citing works
Köybaşı, S., Senkal, C. E., Sundararaj, K. P., Spassieva, S. D., Bielawski, J., Osta, W. A., Day, T. A., Jiang, J. C., Jazwinski, S. M., Hannun, Y. A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406920200 · Cited by 225 · see citing works
Self-citationIn Vivo and in Vitro Reconstitution of Atg8 Conjugation Essential for Autophagy
Ichimura, Y., Imamura, Y., Emoto, K., Umeda, M., Noda, T., & Ohsumi, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405860200 · Cited by 216 · see citing works
Kudo, N., Kumagai, K., Tomishige, N., Yamaji, T., Soichi Wakatsuki, A., Nishijima, M., Hanada, K., & Kato, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709191105 · Cited by 210 · see citing works
Mukhopadhyay, A., Saddoughi, S. A., Song, P., Sultan, I. Y., Ponnusamy, S., Senkal, C. E., Snook, C. F., Arnold, H., Sears, R. C., Hanniui, Y. A., et al. (2008) · The FASEB Journal · doi:10.1096/fj.08-120550 · Cited by 208 · see citing works
Self-citationCeramide Biogenesis Is Required for Radiation-Induced Apoptosis in the Germ Line of C. elegans
Deng, X., Yin, X., Allan, R., Lu, D. D., Maurer, C. W., Haimovitz‐Friedman, A., FUKS, Z. Y., Shaham, S., & Kolesnick, R. N. (2008) · Science · doi:10.1126/science.1158111 · Cited by 207 · see citing works
Ceramide starves cells to death by downregulating nutrient transporter proteins
Guenther, G., Peralta, E. R., Rosales, K. R., Wong, S. Y., Siskind, L. J., & Edinger, A. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802781105 · Cited by 196 · see citing works
Mizutani, Y., Kihara, A., & Igarashi, Y. (2006) · Biochemical Journal · doi:10.1042/bj20060379 · Cited by 179 · see citing works
Protection of C. elegans from Anoxia by HYL-2 Ceramide Synthase
Menuz, V., Howell, K. S., Gentina, S., Epstein, S., Riezman, I., Fornallaz-Mulhauser, M., Hengartner, M. O., Gomez, M., Riezman, H., & Martinou, J. (2009) · Science · doi:10.1126/science.1168532 · Cited by 171 · see citing works
Karahatay, S., Thomas, K., Köybaşı, S., Senkal, C. E., Elojeimy, S. N., Liu, X., Bielawski, J., Day, T. A., Gillespie, M. B., Sinha, D., et al. (2007) · Cancer Letters · doi:10.1016/j.canlet.2007.06.003 · Cited by 170 · see citing works
Self-citationKim, I., & Lemasters, J. J. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00056.2010 · Cited by 154 · see citing works
Self-citationMitochondrial Ceramide-Rich Macrodomains Functionalize Bax upon Irradiation
Lee, H., Rotolo, J. A., Mesicek, J., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019783 · Cited by 151 · see citing works
Sphingosine-1-phosphate phosphohydrolase-1 regulates ER stress-induced autophagy
Lépine, S., Allegood, J. C., Park, M., Dent, P., Milstien, S., & Spiegel, S. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.104 · Cited by 133 · see citing works
Sims, K. H., Haynes, C. A., Kelly, S. L., Allegood, J. C., Wang, E. L., Momin, A. A., Leipelt, M., Reichart, D. R., Glass, C. K., Sullards, M. C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.170621 · Cited by 126 · see citing works
Identification of Dihydroceramide Desaturase as a Direct in Vitro Target for Fenretinide
Rahmaniyan, M., Curley, R. W., Obeid, L. M., Hannun, Y. A., & Kraveka, J. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.250779 · Cited by 125 · see citing works
Necessary Role for the Lag1p Motif in (Dihydro)ceramide Synthase Activity
Spassieva, S., Seo, J.-G., Jiang, J. C., Bielawski, J., Alvarez-Vasquez, F., Jazwinski, S. M., Hannun, Y. A., & Obeid, L. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608092200 · Cited by 121 · see citing works
Self-citationMasud, A. J., Mohapatra, A., Lakhani, S. A., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700077200 · Cited by 101 · see citing works
Senkal, C. E., Ponnusamy, S., Rossi, M. J., Sundararaj, K. P., Szulc, Z. M., Bielawski, J., Bielawska, A. E., Meyer, M., Çobanoğlu, B., Köybaşı, S., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.101949 · Cited by 90 · see citing works
Self-citationSaddoughi, S. A., Garrett-Mayer, E. S., Chaudhary, U. B., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-0930 · Cited by 68 · see citing works
Self-citationA critical role of superoxide anion in selenite-induced mitophagic cell death
Kim, E. H., & Choi, K. S. (2008) · Autophagy · doi:10.4161/auto.5119 · Cited by 57 · see citing works
Tailoring structure–function and targeting properties of ceramides by site-specific cationization
Szulc, Z. M., Bielawski, J., Gracz, H. S., Gustilo, M. M., Mayroo, N., Hannun, Y. A., Obeid, L. M., & Bielawska, A. E. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.07.016 · Cited by 55 · see citing works
Self-citationSpassieva, S. D., Bielawski, J., Anelli, V., & Obeid, L. M. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)34012-3 · Cited by 33 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Shimizu, S. et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nat. Cell Biol. 6, 1221–1228 (2004). · DOI · Paper page
Cited by
Sorted by citations
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 · see citing works
“Ceramides, positioned at the core of sphingolipid metabolism, play several roles that affect multiple steps of macroautophagy, by inhibition of nutrient transporters,(589) by modulation of BCL2-BECN1 association at the level of AKT signaling,(590) and by regulation of mitophagy.(591) The latter function is regulated b…”
Mechanism and medical implications of mammalian autophagy
Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771 · see citing works
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 2,622 · see citing works
Self-consumption: the interplay of autophagy and apoptosis
Mariño, G., Niso-Santano, M., Baehrecke, E. H., & Kroemer, G. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3735 · Cited by 2,172 · see citing works
Sphingolipid metabolism in cancer signalling and therapy
Ogretmen, B. (2018) · Nature Reviews Cancer · doi:10.1038/nrc.2017.96 · Cited by 1,207 · see citing works
Autophagy: Regulator of cell death
Liu, S., Yao, S., Yang, H., Liu, S., & Wang, Y. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06154-8 · Cited by 1,193 · 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
Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors
Johansen, T., & Lamark, T. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.016 · Cited by 700 · see citing works
Mitophagy-dependent necroptosis contributes to the pathogenesis of COPD
Mizumura, K., Cloonan, S. M., Nakahira, K., Bhashyam, A. R., Cervo, M., Kitada, T., Glass, K., Owen, C. A., Mahmood, A., Washko, G. R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74985 · Cited by 611 · see citing works
“Emerging studies have suggested that mitophagy may be deleterious in a context-specific manner (15).”
BackgroundMitophagy, Mitochondrial Homeostasis, and Cell Fate
Ma, K., Chen, G., Li, W., Kepp, O., Zhu, Y., & Chen, Q. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00467 · Cited by 609 · see citing works
“Thus, LC3– ceramide interactions provoked by ceramide treatment induce mitophagy and can progress to autophagic cell death in human cancer cells (Sentelle et al., 2012).”
BackgroundBasit, F., van Oppen, L. M. P. E., Schöckel, L., Bossenbroek, H. M., Vries, S. E. V. E., Hermeling, J. C., Grefte, S., Kopitz, C., Héroult, M., Willems, P. H. G. M., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.133 · Cited by 569 · see citing works
Emerging views of mitophagy in immunity and autoimmune diseases
Xu, Y., Shen, J., & Ran, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1603547 · Cited by 521 · see citing works
“Similarly, ceramide (waxy lipid molecules) engages mitophagic machinery through interaction with LC3, leading to inhibition of mitochondrial function and oxygen consumption in tumor cells [67].”
BackgroundSelective autophagy of intracellular organelles: Recent research advances
Li, W., He, P., Huang, Y., Li, Y.-F., Lu, J., Li, M., Kurihara, H., Luo, Z., Meng, T., Onishi, M., et al. (2020) · Theranostics · doi:10.7150/thno.49860 · Cited by 510 · see citing works
“Additionally, ceramide, a bioactive sphingolipid, has been identified as a selective receptor for mitophagy by binding directly to the LC3-II protein [60].”
BackgroundSchulte, M. L., Fu, A., Zhao, P., Li, J., Geng, L., Smith, S. T., Kondo, J., Coffey, R. J., Johnson, M. O., Rathmell, J. C., et al. (2018) · Nature Medicine · doi:10.1038/nm.4464 · Cited by 494 · see citing works
Mitochondrial biogenesis and clearance: a balancing act
Ploumi, C., Daskalaki, I., & Tavernarakis, N. (2016) · FEBS Journal · doi:10.1111/febs.13820 · Cited by 465 · see citing works
Mitophagy in degenerative joint diseases
Sun, K., Jing, X., Guo, J., Yao, X., & Guo, F. (2020) · Autophagy · doi:10.1080/15548627.2020.1822097 · Cited by 464 · see citing works
Mitochondrial autophagy: molecular mechanisms and implications for cardiovascular disease
Li, A.-Q., Gao, M., Liu, B.-L., Qin, Y., Chen, L., Liu, H., Wu, H.-Y., & Gong, G. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04906-6 · Cited by 418 · see citing works
“Drp1 knockdown disrupts ceramide localization in OMM and autophagolysosomes recruitment in tumor cells [78].”
BackgroundMechanisms 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
Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 396 · see citing works
“In addition to protein mitophagy receptors, the lipids ceramide and cardiolipin, when localized to the OMM can directly bind LC3 and engage mitophagy [69, 70].”
BackgroundMitophagy: 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 · see citing works
The emerging, multifaceted role of mitophagy in cancer and cancer therapeutics
Panigrahi, D. P., Praharaj, P. P., Bhol, C. S., Mahapatra, K. K., Patra, S., Behera, B. P., Mishra, S. R., & Bhutia, S. K. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.07.015 · Cited by 374 · see citing works
Sphingolipids: regulators of crosstalk between apoptosis and autophagy
Young, M. M., KESTER, M. A., & Wang, H. (2012) · Journal of Lipid Research · doi:10.1194/jlr.r031278 · Cited by 329 · see citing works
The pharmacological regulation of cellular mitophagy
Georgakopoulos, N., Wells, G., & Campanella, M. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2287 · Cited by 318 · see citing works
Caenorhabditis elegans pathways that surveil and defend mitochondria
Liu, Y., Samuel, B. S., Breen, P. C., & Ruvkun, G. (2014) · Nature · doi:10.1038/nature13204 · Cited by 309 · see citing works
Autophagy-dependent cell death—where.; how and why a cell eats itself to death
Bialik, S., Dasari, S. K., & Kimchi, A. (2018) · Journal of Cell Science · doi:10.1242/jcs.215152 · Cited by 295 · see citing works
“In this system, the introduction of a C18 ceramide analog, or overexpression of ceramide synthase 1, led to mitophagy and caspase-independent cell death (Sentelle et al., 2012).”
BackgroundResultInfluentialMitochondrial lipid trafficking
Tatsuta, T., Scharwey, M., & Langer, T. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.07.011 · Cited by 286 · see citing works
Czubowicz, K., Jęśko, H. M., Wencel, P. L., Lukiw, W. J., & Strosznajder, R. P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1448-3 · Cited by 285 · see citing works
Role and Mechanisms of Mitophagy in Liver Diseases
Ma, X., McKeen, T., Zhang, J., & Ding, W. (2020) · Cells · doi:10.3390/cells9040837 · Cited by 279 · see citing works
“In addition to CL, ceramide, a bioactive sphingolipid, directly binds LC3 to recruit autophagosomes to the mitochondria resulting in cell death, likely due to the induction of lethal mitophagy in cancer cells [63].”
BackgroundMitochondrial degradation: Mitophagy and beyond
Uoselis, L., Nguyen, T. N., & Lazarou, M. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.08.021 · Cited by 270 · see citing works
Mitochondrial quality control in health and in Parkinson’s disease
Eldeeb, M. A., Thomas, R. A., Ragheb, M. A., Fallahi, A., & Fon, E. A. (2022) · Physiological Reviews · doi:10.1152/physrev.00041.2021 · Cited by 276 · see citing works
Mitophagy in Alzheimer’s Disease and Other Age-Related Neurodegenerative Diseases
Cai, Q., & Jeong, Y. Y. (2020) · Cells · doi:10.3390/cells9010150 · Cited by 263 · see citing works
“Additionally, upon Drp1-mediated mitochondrial fission, ceramide was shown to promote autophagic recruitment of mitochondria through direct interaction of ceramide with LC3B-II [71].”
BackgroundMitophagy in Cancer: A Tale of Adaptation
Vara‐Pérez, M., Felipe‐Abrio, B., & Agostinis, P. (2019) · Cells · doi:10.3390/cells8050493 · Cited by 256 · see citing works
“Additionally, ceramides -sphingolipids present in the OMM- can bind LC3B-II to target the mitochondria for degradation upon DRP1-mediated mitochondrial fragmentation [75].”
BackgroundMitophagy and mitochondrial integrity in cardiac ischemia-reperfusion injury
Yang, M., Linn, B. S., Zhang, Y., & Ren, J. T. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.05.007 · Cited by 250 · see citing works
Serine Availability Influences Mitochondrial Dynamics and Function through Lipid Metabolism
Gao, X., Lee, K., Reid, M. A., Sanderson, S. M., Qiu, C., Li, S., Liu, J., & Locasale, J. W. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.017 · Cited by 249 · see citing works
“Cells were divided as previously described (Karbowski et al., 2006) into three categories: “Normal” with >90% of mitochondria forming elongated interconnected networks, “Intermediate” with mixed tubular and short mitochondria, and “Fragmented” with >90% short punctiform mitochondria.”
Regulation of PRKN-independent mitophagy
Terešak, P., Lapão, A., Subic, N., Boya, P., Elazar, Z., & Simonsen, A. (2021) · Autophagy · doi:10.1080/15548627.2021.1888244 · Cited by 250 · see citing works
“In vitro studies using CL-agarose beads showed that DNM1L has a strong binding affinity to CL [135] and cooperate to promote mitochondrial division [140].”
BackgroundInfluentialMitophagy in tumorigenesis and metastasis
Poole, L. P., & Macleod, K. F. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03774-1 · Cited by 250 · see citing works
The Role of Mitophagy in Innate Immunity
Gkikas, I., Palikaras, K., & Tavernarakis, N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01283 · Cited by 244 · see citing works
“To this direction, shortage of mitochondrial population due to induction or persistent mitophagy has also been reported (140, 157, 158).”
BackgroundCeramide is metabolized to acylceramide and stored in lipid droplets
Senkal, C. E., Salama, M. F., Snider, A. J., Allopenna, J. J., Rana, N. A., Koller, A., Hannun, Y. A., & Obeid, L. M. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.02.010 · Cited by 237 · see citing works
“Ceramide, the central molecule in the sphingolipid pathway, regulates various cellular responses such as growth arrest, senescence, apoptosis, and autophagy (Hannun and Obeid, 2008; Mullen et al., 2012; Russo et al., 2012; Sentelle et al., 2012).”
BackgroundSelf-citationMetabolic features of the cell danger response
Naviaux, R. K. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.08.006 · Cited by 235 · see citing works
Law, B. A., Liao, X., Moore, K. S., Southard, A., Roddy, P. L., Ji, R., Szulc, Z. M., Bielawska, A., Schulze, P. C., & Cowart, L. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700300r · Cited by 222 · see citing works
Self-citationNo Parkin Zone: Mitophagy without Parkin
Villa, E., Marchetti, S., & Ricci, J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.07.004 · Cited by 221 · see citing works
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
Chu, C. T. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.015 · Cited by 218 · see citing works
A guide to the regulation of selective autophagy receptors
Gubaš, A., & Đikić, I. (2021) · FEBS Journal · doi:10.1111/febs.15824 · Cited by 215 · see citing works
Outstanding Questions in Mitophagy: What We Do and Do Not Know
Montava‐Garriga, L., & Ganley, I. G. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.032 · Cited by 209 · see citing works
Dany, M., Gencer, S., Nganga, R., Thomas, R. J., Oleinik, N. V., Baron, K. D., Szulc, Z. M., Ruvolo, P. P., Kornblau, S. M., Andreeff, M., et al. (2016) · Blood · doi:10.1182/blood-2016-04-708750 · Cited by 204 · see citing works
Self-citationGuo, X., Sun, X., Hu, D., Wang, Y.-J., Fujioka, H., Vyas, R., Chakrapani, S., Joshi, A. U., Luo, Y., Mochly-Rosen, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms12646 · Cited by 200 · see citing works
The multifaceted regulation of mitophagy by endogenous metabolites
Zhang, T., Liu, Q., Gao, W., Sehgal, S. A., & Wu, H. (2021) · Autophagy · doi:10.1080/15548627.2021.1975914 · Cited by 207 · see citing works
“The C18-ceramide can localize on mitochondria, where it binds to MAP1LC3 and mediates the phagophore engulfing mitochondria for mitophagy [156,157].”
BackgroundMitochondria as Cellular and Organismal Signaling Hubs
Shen, K., Pender, C. L., Bar‐Ziv, R., Zhang, H., Wickham, K., Willey, E., Durieux, J., Ahmad, Q., & Dillin, A. G. (2022) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120420-015303 · Cited by 203 · see citing works
The role of ceramides in metabolic disorders: when size and localization matters
Turpin-Nolan, S. M., & Brüning, J. C. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0320-5 · Cited by 196 · see citing works
Chen, Y., Chen, H., Wang, K., Zhang, L., Huang, Z., Liu, J., Zhang, Z., Luo, M., Lei, Y., Peng, Y., et al. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.09.022 · Cited by 192 · see citing works
Mitochondrial quality control as a key determinant of cell survival
Sedlackova, L., & Korolchuk, V. I. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.12.012 · Cited by 186 · see citing works
Emerging role of mitophagy in human diseases and physiology
Um, J., & Yun, J. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.6.056 · Cited by 181 · see citing works
“apoptosis and senescence, induces mitophagy (76).”
Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges
Yu, R., Lendahl, U., Nistér, M., & Zhao, J. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00374 · Cited by 173 · see citing works
“For instance, ceramide (a bioactive sphingolipid) in the MOM is found to interact with LC3B-II and trigger lethal mitophagy through the selective targeting of LC3B-II-containing autophagosomes to mitochondria (232).”
BackgroundDiverse Functions of Ceramide in Cancer Cell Death and Proliferation
Saddoughi, S. A., & Öğretmen, B. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-394274-6.00002-9 · Cited by 176 · see citing works
Doxorubicin‐induced cardiomyocyte death is mediated by unchecked mitochondrial fission and mitophagy
Catanzaro, M. P., Weiner, A., Kaminaris, A., Li, C., Cai, F., Zhao, F., Kobayashi, S., Kobayashi, T., Huang, Y., Sesaki, H., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201802663r · Cited by 175 · see citing works
Shen, Y., Guerra‐Librero, A., Fernández-Gil, B. I., Florido, J., García‐López, S., Martínez-Ruiz, L., Mendivil‐Perez, M., Soto‐Mercado, V., Acuña-Castroviejo, D., Ortega‐Arellano, H. F., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12461 · Cited by 171 · see citing works
Hernández‐Tiedra, S., Fabriàs, G., Dávila, D., Salanueva, Í. J., Casas, J., Montes, L. R., Antón, Z., García-Taboada, E., Salazar‐Roa, M., Lorente, M., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1213927 · Cited by 162 · see citing works
“It is worth noting that ceramides had been previously implicated in autophagy-associated cell death via induction of lethal mitophagy.(44) However, we did not find a significant increase in mitophagy upon treatment with THC (data not shown) indicating that this mechanism is not responsible for the stimulation of autop…”
BackgroundInfluentialCeramide and the mitochondrial respiratory chain
Kogot‐Levin, A., & Saada, A. (2013) · Biochimie · doi:10.1016/j.biochi.2013.07.027 · Cited by 156 · see citing works
Muscle sphingolipids during rest and exercise: a C18:0 signature for insulin resistance in humans
Bergman, B. C., Brozinick, J. T., Strauss, A., Bacon, S., Kerege, A., Bui, H. H., Sanders, P., Siddall, P., Wei, T., Thomas, M. K., et al. (2016) · Diabetologia · doi:10.1007/s00125-015-3850-y · Cited by 148 · see citing works
Selvam, S. P., Palma, R. M. D., Oaks, J. J., Oleinik, N. V., Peterson, Y. K., Stahelin, R. V., Skordalakes, E., Ponnusamy, S., Garrett-Mayer, E. S., Smith, C. D., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa4998 · Cited by 150 · see citing works
Self-citationHuang, S., Lü, W., Ge, D., Meng, N., Li, Y., Su, L., Zhang, S., Zhang, Y., Zhao, B., & Miao, J. (2015) · Autophagy · doi:10.1080/15548627.2015.1106663 · Cited by 149 · see citing works
“Furthermore, excessive mitophagy induced by CERS1 is lethal and leads to tumor suppression.(26,47) TGFB2-OT1 downregulation by 3BDO increased MIR3960 levels and reduced those of CERS1, whereas TGFB2-OT1 overexpression downregulated MIR3960 levels and increased the CERS1 protein level (Fig.”
BackgroundThe Role of Mitochondrial Dynamics and Mitophagy in Carcinogenesis, Metastasis and Therapy
Wang, Y., Liu, H., Cao, Y., Zhang, L., Huang, F., & Yi, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00413 · Cited by 149 · see citing works
Increased de novo ceramide synthesis and accumulation in failing myocardium
Ji, R., Akashi, H., Drosatos, K., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.96203 · Cited by 148 · see citing works
Lee, J. K., Jin, H. K., Park, M. H., Kim, B.-R., Lee, P. H., Nakauchi, H., Carter, J., He, X., Schuchman, E. H., & Bae, J. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20132451 · Cited by 147 · see citing works
Hou, X., Fiesel, F. C., Truban, D., Castanedes Casey, M., Lin, W.-L., Soto, A. I., Tacik, P., Rousseau, L. G., Diehl, N. N., Heckman, M. G., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1461294 · Cited by 147 · see citing works
“These include different receptor[46] and lipid-mediated [47,48] pathways that recruit phagophores independent of ubiquitin via direct binding to MAP1LC3A family members.”
BackgroundLong non-coding RNAs involved in autophagy regulation
Yang, L., Wang, H., Shen, Q., Feng, L., & Jin, H. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.464 · Cited by 141 · see citing works
“increased to induce mitophagy (a class of selective autophagy targeting dysfunctional mitochondria) by directly interacting with LC3-II-containing autophagolysosomes upon Drp1dependent mitochondrial fission.(89,91) In summary, ectopic expression of TGFB2-OT1 induced by VEC inflammation triggers activates autophagy via…”
BackgroundPi, H., Xu, S., Zhang, L., Guo, P., Li, Y., Xie, J., Tian, L., He, M., Lu, Y., Li, M., et al. (2013) · Autophagy · doi:10.4161/auto.25665 · Cited by 139 · see citing works
“Mitophagy targets small, round mitochondria for digestion and elimination, whereas mitochondrial elongation can protect the mitochondria from autophagic degradation and can also sustain the ATP levels.(15,16,23) In the present study, we proposed an intriguing mechanism whereby cadmium-induced hepatotoxicity may arise…”
BackgroundInfluentialCeramides in Skin Health and Disease: An Update
Uchida, Y., & Park, K. (2021) · American Journal of Clinical Dermatology · doi:10.1007/s40257-021-00619-2 · Cited by 138 · see citing works
Prieto‐Domínguez, N., Ordóñez, R., Fernández, A., Méndez‐Blanco, C., Baulies, A., García‐Ruiz, C., Fernández-Checa, J. C., Mauriz, J. L., & González‐Gallego, J. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12358 · Cited by 137 · see citing works
A selective inhibitor of ceramide synthase 1 reveals a novel role in fat metabolism
Turner, N. A., Lim, X. Y., Toop, H. D., Osborne, B., Brandon, A. E., Taylor, E. N., Fiveash, C. E., Govindaraju, H., Teo, J. D., McEwen, H. P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05613-7 · Cited by 138 · see citing works
Increased de novo ceramide synthesis and accumulation in failing myocardium
Ji, R., Akashi, H., Drosatos, K., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.82922 · Cited by 136 · see citing works
Wang, J., Gao, S., Wang, S., Xu, Z., & Wei, L. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s165699 · Cited by 134 · see citing works
“Sentelle et al showed that mitophagy induction promotes tumor cell death via a mechanism involving autophagy.(36) To investigate the specific role of PINK1/ Parkin-mediated mitophagy in ZnO NP-induced toxicity, we transfected cells with GFP-LC3 to locate the autophagosomes and used the red fluorescent PINK1 puncta to…”
The mitochondrial unfolded protein response–synchronizing genomes
Jovaisaite, V., & Auwerx, J. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.003 · Cited by 131 · see citing works
Abuhusain, H. J., Matin, A., Qiao, Q., Shen, H. M., Kain, N., Day, B. W., Stringer, B. W., Daniels, B. J., Laaksonen, M. A., Teo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494740 · Cited by 132 · see citing works
Mitophagy-driven metabolic switch reprograms stem cell fate
Naik, P. P., Birbrair, A., & Bhutia, S. K. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2922-9 · Cited by 130 · see citing works
The enigma of ceramide synthase regulation in mammalian cells
Wegner, M.-S., Schiffmann, S., Parnham, M. J., Geißlinger, G., & Grösch, S. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.03.006 · Cited by 130 · see citing works
Mitophagy: Link to cancer development and therapy
Kulikov, A. V., Luchkina, E. A., Gogvadze, V. G., & Zhivotovsky, B. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.088 · Cited by 128 · see citing works
Wolbachia Modulates Lipid Metabolism in Aedes albopictus Mosquito Cells
Molloy, J., Sommer, U., Viant, M. R., & Sinkins, S. P. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.00275-16 · Cited by 130 · see citing works
“This hypothesis fits with our current knowledge that activation of autophagy can reduce Wolbachia bacterial density (30) and that accumulated ceramides are able to activate both autophagic and apoptotic pathways by interacting with the mTOR pathway (62, 63) and have been shown to target autophagosomes to mitochondria…”
Ceramide induced mitophagy and tumor suppression
Dany, M., & Öğretmen, B. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.039 · Cited by 129 · see citing works
Mitochondrial quality control in intervertebral disc degeneration
Song, Y., Lu, S., Geng, W., Feng, X., Luo, R., Li, G., & Cao, Y. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00650-7 · Cited by 131 · see citing works
Contribution of specific ceramides to obesity-associated metabolic diseases
Hammerschmidt, P., & Brüning, J. C. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04401-3 · Cited by 128 · see citing works
“In the same study, exogenously applied C16:0 ceramides also localized to mitochondria, where they decreased mitochondrial oxygen-consumption rate and induced mitophagy [181].”
Backgroundde la Mata, M., Cotán, D., Oropesa-Ávila, M., Garrido-Maraver, J., Cordero, M. D., Villanueva Paz, M., Delgado Pavón, A., Alcocer-Gómez, E., de Lavera, I., Ybot-González, P., et al. (2015) · Scientific Reports · doi:10.1038/srep10903 · Cited by 126 · see citing works
Inhibition of acid sphingomyelinase by tricyclic antidepressants and analogons
Beckmann, N., Sharma, D., Gulbins, E., Becker, K. A., & Edelmann, B. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00331 · Cited by 127 · see citing works
“Some ceramide-interacting proteins are already identified, for instance kinase suppressor of Ras (KSR) (Zhang et al., 1997; Zhou et al., 2002), ceramide-activated protein phosphatase (CAPP) (Dobrowsky et al., 1993; Wolff et al., 1994; Saddoughi et al., 2013), protein kinase C (PKC)-alpha, and -delta (Huwiler et al., 1…”
Gosejacob, D., Jäger, P. S., Dorp, K. V., Frejno, M., Carstensen, A., Köhnke, M., Degen, J., Dörmann, P., & Hoch, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691212 · Cited by 127 · see citing works
“More directly, mitochondrial C18:0and C16:0-ceramides interact with LC3B to recruit autophagosomes to mitochondria to induce mitophagy (68).”
BackgroundHernandez‐Corbacho, M. J., Salama, M., Canals, D., Senkal, C. E., & Obeid, L. M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.09.019 · Cited by 126 · see citing works
Self-citationDendrogenin A drives LXR to trigger lethal autophagy in cancers
Segala, G., David, M., de Medina, P., Poirot, M. C., Serhan, N., Vergez, F., Mougel, A., Saland, E., Carayon, K., Leignadier, J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01948-9 · Cited by 125 · see citing works
Hu, X., Li, Z., Lin, R., Shan, J.-Q., Yu, Q., Wang, R., Liao, L., Yan, W., Zhen, W., Shang, L., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.634690 · Cited by 127 · see citing works
Pienimaeki‐Roemer, A., Kuhlmann, K., Böttcher, A., Konovalova, T., Black, A., Orsó, E., Liebisch, G., Ahrens, M., Eisenacher, M., Meyer, H. E., et al. (2014) · Transfusion · doi:10.1111/trf.12874 · Cited by 126 · see citing works
“2), which incorporates in the outer membrane of mitochondria, forming permeabilizing pores(55) or promoting autophagosome assembly on damaged mitochondrial membrane.(56) Also the mitochondrial lipid marker CL(57) (Fig.”
BackgroundCeramides and mitochondrial fatty acid oxidation in obesity
Fucho, R., Casals, N., Serra, D., & Herrero, L. (2016) · The FASEB Journal · doi:10.1096/fj.201601156r · Cited by 124 · see citing works
Molecular Mechanisms and Regulation of Mammalian Mitophagy
Choubey, V., Zeb, A., & Kaasik, A. (2021) · Cells · doi:10.3390/cells11010038 · Cited by 123 · see citing works
Meyer, N. E., Zielke, S., Michaelis, J. B., Linder, B., Warnsmann, V., Rakel, S., Osiewacz, H. D., Fulda, S., Mittelbronn, M. G. A., Münch, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1476812 · Cited by 122 · see citing works
Molecular Regulation Mechanisms and Interactions Between Reactive Oxygen Species and Mitophagy
Fan, P., Xie, X.-H., Chen, C., Peng, X., Zhang, P., Yang, C. H., & Wang, Y. (2018) · DNA and Cell Biology · doi:10.1089/dna.2018.4348 · Cited by 120 · see citing works
“Ceramide can increase cancer cell death and chemotherapy sensitivity through inducing the formation of lipidated LC3 and then promoting mitophagy in cancer cells (Sentelle et al. , 2012; Dany et al. , 2016).”
Autophagy paradox and ceramide
Jiang, W., & Öğretmen, B. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.09.005 · Cited by 118 · see citing works
Self-citationMitochondrial quality control: Easy come, easy go
Stotland, A. B., & Gottlieb, R. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.041 · Cited by 118 · see citing works
“Sphingolipids are synthesized in the ER but when ceramides are delivered to the OMM, they serve as important binding sites for LC3-II, thereby mediating mitophagy [109].”
BackgroundMitochondria as intracellular signaling platforms in health and disease
Tan, J. X., & Finkel, T. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202002179 · Cited by 119 · see citing works
Advances in determining signaling mechanisms of ceramide and role in disease
Stith, J. L., Velazquez, F. N., & Obeid, L. M. (2019) · Journal of Lipid Research · doi:10.1194/jlr.s092874 · Cited by 116 · see citing works
“tophagosomes to mitochondria to induce lethal mitophagy (19).”
BackgroundMitophagy: A novel perspective for insighting into cancer and cancer treatment
Song, C., Pan, S., Zhang, J., Li, N., & Geng, Q. (2022) · Cell Proliferation · doi:10.1111/cpr.13327 · Cited by 115 · see citing works
“Activation of the ceramide stress pathway can induce mitophagy to promote cell death in HNSCC.(150) In malignant gliomas, ceramide can upregulate BNIP3 expression to induce mitophagy and cause cancer cell death.”
BackgroundLongo, M., Meroni, M., Paolini, E., Macchi, C., & Dongiovanni, P. (2021) · Metabolism · doi:10.1016/j.metabol.2021.154708 · Cited by 112 · see citing works
UPRmt-mediated cytoprotection and organismal aging
Schulz, A. M., & Haynes, C. M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.03.008 · Cited by 110 · see citing works
“Intriguingly, ceramide is known to accumulate on damaged mitochondria and is also required for early events in mitophagy [99] suggesting a potential role in coordinating both pathways.”
BackgroundLC3 subfamily in cardiolipin-mediated mitophagy: a comparison of the LC3A, LC3B and LC3C homologs
Iriondo, M. N., Etxaniz, A., Varela, Y. R., Ballesteros, U., Hervás, J. H., Montes, L. R., Goñi, F. M., & Alonso, A. (2022) · Autophagy · doi:10.1080/15548627.2022.2062111 · Cited by 113 · see citing works
“Lipids, such as ceramide [15] or cardiolipin [16], can also serve as damaged mitochondrial signals/receptors.”
Background
- Authors
- Sentelle, R. D., Senkal, C. E., Jiang, W., Ponnusamy, S., Gencer, S., Panneer Selvam, S., Ramshesh, V. K., Peterson, Y. K., Lemasters, J. J., Szulc, Z. M., Bielawski, J., & Ogretmen, B.
- Affiliations
- Medical University of South Carolina (US)
- Venue
- Nature Chemical Biology
- Published
- 2012-08-26
- Volume
- 8
- Issue
- 10
- Pages
- 831-838
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC3689583
- OpenAlex
- W1981224101
- Cited by
- 539
- References
- 44
- Citations by year
- 2026: 36 · 2025: 44 · 2024: 50 · 2023: 56 · 2022: 35 · 2021: 47 · 2020: 38 · 2019: 37 · 2018: 48 · 2017: 41 · 2016: 32 · 2015: 31 · 2014: 27 · 2013: 15 · 2012: 2
- FWCI
- 17.96
- Type
- journal article
- Language
- en
- Update notices
- erratum (2012-11-26)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1c06rr015455-01a1)
- National Institute on Alcohol Abuse and Alcoholism (P50AA011605, 1-P50-AA11605)
- National Cancer Institute (CA088932, R01CA088932, CA097165, P30CA138313)
- National Institute of Diabetes and Digestive and Kidney Diseases (5P30 DK 34987, P30DK034987)
- National Institute of Dental and Craniofacial Research (DE-016572, R01DE016572)
- National Center for Research Resources (C06 RR-015455)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ceramide, mitophagy, autophagy, LC3B-II, LC3B lipidation, CERS1, autophagic cell death, Drp1, mitochondrial fission, autophagolysosomes, mitochondrial targeting, oxygen consumption, sodium selenite, tumor suppression, cancer cells
- MeSH terms
- Autophagy, Ceramides, Humans, Lipids, Phagosomes, Cell Death, Microscopy, Confocal, Cell Line, Tumor, Mitophagy
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