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Nix is a selective autophagy receptor for mitochondrial clearance
Open accessAbstract
Autophagy is the cellular homeostatic pathway that delivers large cytosolic materials for degradation in the lysosome. Recent evidence indicates that autophagy mediates selective removal of protein aggregates, organelles and microbes in cells. Yet, the specificity in targeting a particular substrate to the autophagy pathway remains poorly understood. Here, we show that the mitochondrial protein Nix is a selective autophagy receptor by binding to LC3/GABARAP proteins, ubiquitin-like modifiers that are required for the growth of autophagosomal membranes. In cultured cells, Nix recruits GABARAP-L1 to damaged mitochondria through its amino-terminal LC3-interacting region. Furthermore, ablation of the Nix:LC3/GABARAP interaction retards mitochondrial clearance in maturing murine reticulocytes. Thus, Nix functions as an autophagy receptor, which mediates mitochondrial clearance after mitochondrial damage and during erythrocyte differentiation.
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“Mitophagy can also occur through Parkin-independent pathways.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [140]
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BackgroundRhes, a striatal-enriched protein, promotes mitophagy via Nix
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BackgroundULK1, Mammalian Target of Rapamycin, and Mitochondria: Linking Nutrient Availability and Autophagy
Kundu, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3809 · Cited by 48
“Moreover, its mitochondrial localization and ability to directly interaction with Atg8 homologs suggest that it is involved in targeting the organelle for degradation by autophagy (38).”
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The “mitochondrial stress responses”: the “Dr. Jekyll and Mr. Hyde” of neuronal disorders
Rimessi, A., Patergnani, S., Morciano, G., Carinci, M., Leo, S., & Pinton, P. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.339473 · Cited by 41
“In line with this, NIP3like protein X (NIX/BNIP3L) is another OMM-resident protein that mediating to specific WXXL-like motif may bind LC3 to sequester mitochondria (Novak et al., 2010; Yuan et al., 2017).”
BackgroundCentral role of Nix in the autophagic response to ochratoxin A
Shen, X. L., Zhang, B., Liang, R., Cheng, W., Xu, W., Luo, Y., Zhao, C., & Huang, K. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.04.017 · Cited by 39
Role of mitophagy in the neurodegenerative diseases and its pharmacological advances: A review
Wang, Q., Xue, H., Yue, Y., Hao, S., Huang, S., & Zhang, Z. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1014251 · Cited by 38
“NIX, which is involved in the clearance of mitochondria during mammalian erythrocyte maturation, plays an important role in mitophagy (Novak et al., 2010).”
BackgroundUfmylation reconciles salt stress-induced unfolded protein responses via ER-phagy in Arabidopsis
Li, B., Niu, F., Zeng, Y., Tse, M. K., Deng, C., Hong, L., Gao, S., Lo, S. W., Cao, W., Huang, S., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208351120 · Cited by 38
“ATG8, the ubiquitin-like protein that decorates the autophagosomal double membranes and recruits cargoes or receptors during autophagosome biogenesis, is commonly used as a bait for identifying novel autophagy regulators and receptors in mammals (40).”
BackgroundSkawratananond, S., Xiong, D. X., Zhang, C., Tonk, S. S., Pinili, A., Delacruz, B., Pham, P., Smith, S. C., Navab, R., & Reddy, P. H. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102732 · Cited by 41
Hammerling, B. C., Shires, S. E., Leon, L. J., Cortez, M. Q., & Gustafsson, Å. B. (2017) · Small GTPases · doi:10.1080/21541248.2017.1342749 · Cited by 36
“therefore bypassing the need for Parkin and ubiquitination.(8,11,28) Interestingly, our data suggest that BNIP3 can also target mitochondria to the early endosomes, but how this occurs is still unclear.”
BackgroundPEX5 regulates autophagy via the mTORC1-TFEB axis during starvation
Eun, S. Y., Lee, J. N., Nam, I.-K., Liu, Z., So, H., Choe, S., & Park, R. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-017-0007-8 · Cited by 38
Autophagy Roles in Genome Maintenance
Ambrosio, S., & Majello, B. (2020) · Cancers · doi:10.3390/cancers12071793 · Cited by 38
The Loss of Mitochondrial Quality Control in Diabetic Kidney Disease
Dai, W., Lu, H., Chen, Y., Yang, D., Sun, L., & He, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.706832 · Cited by 39
“The receptor in the ubiquitinindependent pathway is made up of Bnip3 (Hamacher-Brady et al., 2007; Zhu et al., 2013), its homolog Bnip3L/Nix (Schweers et al., 2007; Novak et al., 2010), FUNDC1 (Liu et al., 2012) and Bcl2L13 (Murakawa et al., 2015), which localize to the OMM.”
Autophagy: Mechanisms, regulation, and its role in tumorigenesis
Parkhitko, A. A., Favorova, O. O., & Henske, E. P. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913040044 · Cited by 39
Deepak, K., Roy, P., Das, C. K., Mukherjee, B., & Mandal, M. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119752 · Cited by 39
Sargsyan, A., Cai, J., Fandino, L. B., Labasky, M. E., Forostyan, T., Colosimo, L. K., Thompson, S. J., & Graham, T. E. (2015) · Scientific Reports · doi:10.1038/srep12397 · Cited by 36
Bcl-2 family members: Essential players in skin cancer
Nys, K., & Agostinis, P. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.01.031 · Cited by 38
Autophagy as a target for hematological malignancy therapy
Dong, Z., Liang, S., Hu, J., Jin, W., Zhan, Q., & Zhao, K. (2016) · Blood Reviews · doi:10.1016/j.blre.2016.04.005 · Cited by 37
Ryabovol, V., & Minibayeva, F. V. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916040052 · Cited by 37
“Another large group of AIM proteins includes molecules (NBR, p62, Nix/Binp3L, etc.) that participate in selective removal of cell components [85].”
BackgroundInfluentialLi, Y., Liu, Z., Zhang, Y., Zhao, Q., Wang, X., Lü, P., Zhang, H., Wang, Z., Dong, H., & Zhang, Z. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3536 · Cited by 37
“Mitophagy is mainly mediated by three signaling pathways, namely, Parkin, Nix and FUNDC1 (23-25).”
BackgroundThe intersection of exercise and aging on mitochondrial protein quality control
Zhang, Y., Oliveira, A. N., & Hood, D. A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2019.110824 · Cited by 40
Eating the unknown: Xenophagy and ER-phagy are cytoprotective defenses against pathogens
Reggio, A., Buonomo, V., & Grumati, P. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112276 · Cited by 38
“Specifically, autophagy receptors identify an “ eat-me ” signal, mostly composed of ubiquitin chains, on cargo (e.i, p62, OPTN) [27] [ – ] [29] or are themselves resident proteins of the targeted organelle (e.i, NIX, FAM134B) [30,31].”
Mitophagy in Diabetic Kidney Disease
Zhang, X., Feng, J., Li, X., Wu, D., Wang, Q., Li, S., & Shi, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.778011 · Cited by 38
Overexpression of Rcan1-1L Inhibits Hypoxia-Induced Cell Apoptosis through Induction of Mitophagy
Sun, L., Hao, Y., An, R. F., Li, H., Xi, C., & Shen, G. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.0103 · Cited by 36
“Nix and Bnip3 have been reported to bind to microtubule-associated protein light chain 3 (LC3) for autophagolysosome membrane formation during autophagy and mediate the entry of the mitochondrion into an autophagosome (Novak et al., 2010; Zhang and Ney, 2009).”
BackgroundRedox modification of proteins as essential mediators of CNS autophagy and mitophagy
Lizama, B. N., & McLaughlin, B. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.06.007 · Cited by 38
“Notably, no metazoan homologues of Atg32 have been identified, but other molecules that work with Atg homologues in eukaryotic organisms such as NIX (also called BNIP3L), integrate redox sensitivity with organelle degradation mediated by Atg8 [68,69].”
BackgroundInfluentialHallmarks and Molecular Tools for the Study of Mitophagy in Parkinson’s Disease
Goiran, T., Eldeeb, M. A., Zorca, C. E., & Fon, E. A. (2022) · Cells · doi:10.3390/cells11132097 · Cited by 38
“Furthermore, BNIP3 and NIX have similar N-terminal LIR domains exposed to the cytosol that facilitates LC3s (microtubule-associated protein 1A/1B light chain) interactions for both receptors, or to GABARAP (gamma aminobutyric acid receptor-associated protein) for NIX, leading to the recruitment of autophagosomes and t…”
BackgroundThe interplay between mitophagy and mitochondrial ROS in acute lung injury
Zhong, Y., Xia, S., Wang, G., Liu, Q., Ma, F., Yu, Y., Zhang, Y., Qian, L., Hu, L., & Xie, J. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101920 · Cited by 38
Long, W. S., Zeng, Y., Zheng, B., Li, Y., Wang, Y., Chan, K., She, M., Lu, Y., Cao, C., & Wong, W. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01255 · Cited by 37
Liu, H., Song, Y., Wang, H., Zhou, Y., Xu, M., & Xian, J. (2025) · Phytotherapy Research · doi:10.1002/ptr.8433 · Cited by 37
Diversity in the Regulation of Autophagy and Mitophagy: Lessons from Parkinson's Disease
Chu, C. T. (2011) · Parkinson s Disease · doi:10.4061/2011/789431 · Cited by 34
“Indeed, depolarization-independent, Nix-dependent mitophagy may involve direct interactions of Nix with an LC3 homolog GABARAP [83], indicating alternative signaling for mitochondria recognition during autophagosome formation.”
BackgroundBrennan, L., Disatham, J., & Kantorow, M. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108129 · Cited by 36
“Extensive studies on BNIP3L show that it is required for elimination of mitochondria during reticulocyte differentiation (Novak et al., 2010; Sandoval et al., 2008; Schweers et al., 2007; Zhang and Ney, 2008) and, consistently, fully mature erythrocytes in BNIP3L knockout mice retain mitochondria resulting in dysfunct…”
BackgroundHuman erythroid differentiation requires VDAC1-mediated mitochondrial clearance
Moras, M., Hattab, C., González‐Menéndez, P., Fader, C. M., Dussiot, M., Larghero, J., Kim, C. L. V., Kinet, S., Taylor, N. N., Lefevre, S. D., et al. (2021) · Haematologica · doi:10.3324/haematol.2020.257121 · Cited by 40
Mitochondrial disease, mitophagy, and cellular distress in methylmalonic acidemia
Luciani, A., Denley, M. C. S., Govers, L. P., Sorrentino, V., & Froese, D. S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03934-3 · Cited by 41
Gao, Y., Wang, C., Jiang, D. M., An, G., Jin, F. J., Zhang, J., Han, G., Cui, C., & Jiang, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.994037 · Cited by 37
“The most well-accepted mechanism underlying BNIP3L-mediated mitophagy is through an interaction with proteins from the Atg8 family, by which BNIP3L recruits autophagosomes to targeted mitochondria (Novak et al., 2010).”
BackgroundPassantino, R., Cascio, C., Deidda, I., Galizzi, G., Russo, D., Spedale, G., & Guarneri, P. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.10.030 · Cited by 36
NIX-mediated mitophagy protects against proteinuria-induced tubular cell apoptosis and renal injury
Xu, D., Chen, P., Wang, B., Wang, Y., Miao, N., Yin, F., Cheng, Q., Zhou, Z., Xie, H., Zhou, L., et al. (2019) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00360.2018 · Cited by 35
Targeting of biomolecular condensates to the autophagy pathway
Ma, X., Li, P., & Ge, L. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.08.006 · Cited by 34
Metadata
- Authors
- Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., Reichert, A. S., Terzic, J., Dötsch, V., Ney, P. A., & Dikic, I.
- Affiliations
- Mediterranean Institute for Life Sciences (HR)
- Goethe University Frankfurt (DE)
- St. Jude Children's Research Hospital (US)
- ORCID
- Venue
- The EMBO Reports
- Published
- 2009-12-11
- Volume
- 11
- Issue
- 1
- Pages
- 45-51
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2816619
- OpenAlex
- W2127440157
- Cited by
- 1,309
- References
- 35
- Citations by year
- 2026: 63 · 2025: 77 · 2024: 79 · 2023: 72 · 2022: 81 · 2021: 106 · 2020: 96 · 2019: 86 · 2018: 77 · 2017: 74 · 2016: 85 · 2015: 72 · 2014: 77 · 2013: 63 · 2012: 90
- FWCI
- 44.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft ((EXC 115).)
- Terry Fox Foundation
- National Institutes of Health (CA21765))
- National Cancer Institute (P 30CA 21765, P30CA021765)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK074519, R21DK074519)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- Nix, selective autophagy, mitophagy, autophagy receptors, LC3, GABARAP, LC3-interacting region, mitochondrial clearance, mitochondrial damage, reticulocytes, erythroid differentiation, ubiquitin-like proteins
- MeSH terms
- Autophagy-Related Protein 8 Family, Amino Acid Sequence, Animals, Autophagy, Binding Sites, Cells, Cultured, Chlorocebus aethiops, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Molecular Sequence Data, Protein Binding, Proto-Oncogene Proteins, Receptors, GABA-A, Reticulocytes, Substrate Specificity, Blotting, Western, COS Cells, Amino Acid Motifs, Mitochondrial Proteins, Tumor Suppressor Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, Mice
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