The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Parkin-Independent Mitophagy Controls Chemotherapeutic Response in Cancer Cells
Open accessAbstract
Mitophagy is an evolutionarily conserved process that selectively targets impaired mitochondria for degradation. Defects in mitophagy are often associated with diverse pathologies, including cancer. Because the main known regulators of mitophagy are frequently inactivated in cancer cells, the mechanisms that regulate mitophagy in cancer cells are not fully understood. Here, we identified an E3 ubiquitin ligase (ARIH1/HHARI) that triggers mitophagy in cancer cells in a PINK1-dependent manner. We found that ARIH1/HHARI polyubiquitinates damaged mitochondria, leading to their removal via autophagy. Importantly, ARIH1 is widely expressed in cancer cells, notably in breast and lung adenocarcinomas; ARIH1 expression protects against chemotherapy-induced death. These data challenge the view that the main regulators of mitophagy are tumor suppressors, arguing instead that ARIH1-mediated mitophagy promotes therapeutic resistance.
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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
The landscape of somatic copy-number alteration across human cancers
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The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · cited 1×
“The ubiquitin (Ub) E3 ligase Parkin, which is mutated in recessive familial forms of Parkinson’s disease, is a key mediator of mitochondrial quality control processes (Kitada et al., 1998; Shimura et al., 2000).”
BackgroundDrosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
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Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755 · cited 1×
“It was recently suggested that optineurin and NDP52 are key cargo adaptors for Parkin-mediated mitophagy (Heo et al., 2015; Lazarou et al., 2015; Richter et al., 2016).”
Backgroundp62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
Okatsu, K., Saisho, K., Shimanuki, M., Nakada, K., Shitara, H., Sou, Y., Kimura, M., Sato, S., Hattori, N., Komatsu, M., et al. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01426.x · Cited by 397 · cited 3×
“While p62 was initially shown to be critical for removing depolarized mitochondria by transporting them to autophagosomes, later studies suggested a possible redundancy with the related Ub- and Atg8/LC3II-binding protein NBR1 (Narendra et al., 2010; Okatsu et al., 2010), NDP52 (nuclear domain 10 protein 52, also known…”
BackgroundTwo Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
Scott, D. C., Rhee, D. Y., Duda, D. M., Kelsall, I. R., Olszewski, J. L., Paulo, J. A., de Jong, A., Ovaa, H., Alpi, A. F., Harper, J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.027 · Cited by 229
Cited by
Guidelines 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-citationAmyloid Beta and Phosphorylated Tau-Induced Defective Autophagy and Mitophagy in Alzheimer’s Disease
Reddy, P. H., & Oliver, D. M. (2019) · Cells · doi:10.3390/cells8050488 · Cited by 496
“Ariadne RBR E3 ubiquitin protein ligase 1 (ARIH1) is an E3 ubiquitin protein ligase that targets proteins for autophagy via ubiquitination [103].”
BackgroundLou, G., Palikaras, K., Lautrup, S., Scheibye-Knudsen, M., Tavernarakis, N., & Fang, E. F. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.07.002 · Cited by 452
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
Yao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441
Metadata
- Authors
- Villa, E., Proïcs, E., Rubio-Patiño, C., Obba, S., Zunino, B., Bossowski, J. P., Rozier, R. M., Chiche, J., Mondragón, L., Riley, J. S., Marchetti, S., Verhoeyen, E., Tait, S. W. G., & Ricci, J.-E.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2017-09
- Volume
- 20
- Issue
- 12
- Pages
- 2846-2859
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2755721896
- Cited by
- 313
- References
- 9
- FWCI
- 19.85
- Type
- journal article
- Language
- en
- Open access
- gold
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
