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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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Vives-Bauzá, C., Tocilescu, M. A., deVries, R. L. A., Wolken, D. M. A., Jackson-Lewis, V. R., & Przedborski, S. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)83006-7 · Cited by 20
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“Intriguingly, the predicted architecture of Atg32Δ200–341 more closely resembles the mammalian mitophagy receptors BNIP3 (BCL2 interacting protein 3) and BNIP3L/NIX (BCL2 interacting protein 3 like), with an N-terminal disordered sequence that contains the LIR linked to a single transmembrane helix [33,34].”
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Nezis, I. P. (2012) · International Journal of Cell Biology · doi:10.1155/2012/146767 · Cited by 20
“In mammals, mitophagy was described during the physiological process of red blood cell differentiation and it requires the outer mitochondrial membrane protein NIP3-like protein NIX, which is also binds to LC3 through its LIR motif [42, 43].”
BackgroundUbiquitin signaling in PINK1/Parkin-dependent mitophagy
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“Owing to the homology between NIX and BNIP3, NIX also has an LIR motif and a C-terminal TMD, and can recruit GABARAP-L1 to the damaged mitochondria via the LIR; the recruitment of GABARAP-L1 is essential for Nix-mediated mitochondrial clearance [130].”
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“…underlying Nix-mediate mitophagy such as recognition of dysfunctional mitochondria remains unknown, Nix mediates the isolation of mitochondria into autophagosomes through forming a protein complex with LC3/gamma-aminobutyric acid receptor-associated protein (GABARAP; Novak et al., 2010; Figure 1).”
BackgroundMitophagy-Mediated Tumor Dormancy Protects Cancer Cells from Chemotherapy
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“In addition to the ubiquitination pathway, non-ubiquitin-dependent autophagic pathways involving proteins like NIX, BNIP3, and FUNDC1 also participate in mitochondrial autophagy [8,12–14].”
BackgroundFeng, C., Hu, Z., Zhao, M., Leng, C., Li, G., Yang, F., & Fan, X. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1579507 · Cited by 22
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“Moreover, BNIP3L, which often is present at the outer surface of mitochondria, possesses a WXXL motif that binds to LC3 and its homolog GABARAP (Novak et al., 2010), thereby targeting mitochondria for autophagic destruction.”
BackgroundCrosstalk between Autophagy and RLR Signaling
Ke, P. (2023) · Cells · doi:10.3390/cells12060956 · Cited by 17
Mitophagy-promoting agents and their ability to promote healthy-aging
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ResultBurks, T. N., Marx, R., Powell, L., Rucker, J. J., Bedja, D., Heacock, E., Smith, B. J., Foster, D. B., Kass, D. A., O'Rourke, B. P., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3979 · Cited by 17
“Nix is a protein marker expressed on damaged mitochondria and required for autophagic induction [30].”
BackgroundHyperactivated mitophagy in hematopoietic stem cells
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NIX Mediates Mitophagy in Spinal Cord Injury in Rats by Interacting with LC3
Nie, P., Wang, H., Yu, D., Wu, H., Ni, B., Kong, J., & Zhang, Z. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01082-7 · Cited by 16
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“process by triggering mitochondrial depolarization and mitophagy.(69,70) Although mitophagy is considered to be es-”
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Borbolis, F., & Palikaras, K. (2022) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2022.31 · Cited by 16
“65).”
Mitochondrial dysfunction in heart diseases: Potential therapeutic effects of Panax ginseng
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“All three belong to mitochondrial outer membrane proteins (Novak et al., 2010; Chen et al., 2014; Drake et al., 2017).”
BackgroundZhang, Y., Sun, Y., Shi, J., Xu, P. H., Wang, Y., Liu, J., Gong, X., Wang, Y., Tang, Y., Liu, H., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2402817121 · Cited by 16
“…( 15 – 20 ), the selective autophagy of dysfunctional mitochondria (mitophagy) by the autophagy receptor Nix, FUNDC1, Optineurin, and NDP52 ( 21 – 25 ), the selective autophagy of superfluous endoplasmic reticulum (ER) (ER - phagy) by the autophagy receptor CCPG1, FAM134B, Sec62, and TEX264…”
Tau phosphorylation suppresses oxidative stress-induced mitophagy via FKBP8 receptor modulation
Isei, M. O., Crockett, M., Chen, E., Rodwell‐Bullock, J., Carroll, T., Girardi, P., Nehrke, K. W., & Johnson, G. V. W. (2025) · PLoS ONE · doi:10.1371/journal.pone.0307358 · Cited by 16
Mitophagy in Neurodegenerative Diseases: Mechanisms of Action and the Advances of Drug Discovery
Yang, P., Wen, S., Wang, X., Hu, X., Zhao, M., Wang, A., Wu, Y., Ouyang, L., & Wang, G. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01779 · Cited by 17
Nix Nought Nothing: Fairy tale or real deal
Dorn, G. W. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.09.011 · Cited by 16
“A simultaneous report identified the Nix-GABARAP interaction by yeast twohybrid screen using the autophagy factor Atg8 as bait [31].”
MethodMacia, M. G., Santos‐Ledo, A., Caballero, B., Rubio‐González, A., de Luxán‐Delgado, B., Potes, Y., Rodríguez‐González, S., Boga, J. A., & Coto‐Montes, A. M. (2019) · Scientific Reports · doi:10.1038/s41598-019-54743-5 · Cited by 16
Effects of Mitophagy on Regulatory T Cell Function in Patients With Myasthenia Gravis
Wang, N., Jiang, Y., Karim, M. R., Zhong, P., Sun, Y.-P., Zhang, H.-Y., & Wang, Y.-F. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00238 · Cited by 17
“Mitophagy has been observed as selective autophagy in various physiological processes and diseases, such as reticulocyte development (12).”
BackgroundLehotzky, A., Oláh, J., Fekete, J. T., Szénási, T., Szabó, E., Győrffy, B., Várady, G., & Ovádi, J. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.666026 · Cited by 16
Lin, F., Zhu, Y., & Qin, Z. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-2830-6_12 · Cited by 17
Mitophagy: Critical Role in Atherosclerosis Progression
Chen, Y., Qin, W., Lü, L., Wu, P., & Wei, D. (2022) · DNA and Cell Biology · doi:10.1089/dna.2022.0249 · Cited by 17
“After NIX dimerization through the transmembrane structural domain, two potential LIRs recruit LC3/GABARAP-L1 to induce mitophagy (Novak et al. , 2010).”
Mitophagy Disequilibrium, a Prominent Pathological Mechanism in Metabolic Heart Diseases
Li, Y., Zheng, N., & Ding, X. (2021) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s336882 · Cited by 17
“Ambivero CT, Cilenti L, Main S, Zervos AS. Mulan E3 ubiquitin ligase interacts with multiple E2 conjugating enzymes and participates in mitophagy by recruiting GABARAP.”
BackgroundThe pivotal role of dysregulated autophagy in the progression of non-alcoholic fatty liver disease
Shen, Q., Yang, M., Wang, S., Chen, X., Chen, S., Zhang, R., Xiong, Z., & Leng, Y. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1374644 · Cited by 15
Mitophagy in fibrotic diseases: molecular mechanisms and therapeutic applications
Cui, X. T., Zhou, Z., Tu, H., Wu, J., Zhou, J. P., Yi, Q., Liu, O., & Dai, X. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1430230 · Cited by 17
Chai, G., Mao, Y., Gong, J., Bi, S., Zhang, Y., Wu, J., Liu, Y., Gao, T., Fu, H., Yu, C., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07834-3 · Cited by 17
“The degradation of mitochondria (mitophagy) is regulated by two major pathways: the PINK1/PARKIN pathway and a set of receptor proteins, including FUNDC1, NIX, and BCL2L13 [19, 20].”
The rapidly expanding role of LC3-interacting regions in autophagy
North, B. J., Fracchiolla, D., Ragusa, M. J., Martens, S., & Shoemaker, C. J. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202504076 · Cited by 17
Universal dynamics of mitochondrial networks: a finite-size scaling analysis
Zamponi, N., Zamponi, E., Cannas, S. A., & Chialvo, D. R. (2022) · Scientific Reports · doi:10.1038/s41598-022-14946-9 · Cited by 15
Sharma, R. K., Chafik, A., & Bertolin, G. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00256.2021 · Cited by 16
Merline, R., Roedig, H., Zeng-Brouwers, J., Poluzzi, C., Tascher, G., Michaelis, J. B., López-Mosqueda, J., Rhiner, A., Huber, L. S., Diehl, V., et al. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00493.2022 · Cited by 15
The Role of Alternative Mitophagy in Heart Disease
Nah, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076362 · Cited by 16
“In addition, BNIP3L interacts with Atg8 family proteins through its LIR motif, which is essential for enhancing mitophagy [55].”
BackgroundRole and clinical implication of autophagy in COVID-19
Shan, T., Li, L., Yang, J., & Cheng, Y. (2023) · Virology Journal · doi:10.1186/s12985-023-02069-0 · Cited by 17
Mitophagy in tumor: foe or friend？
Li, L., & Hu, F. (2023) · Endokrynologia Polska · doi:10.5603/ep.95652 · Cited by 15
Mechanistic insights into the interactions of TAX1BP1 with RB1CC1 and mammalian ATG8 family proteins
Zhang, M., Wang, Y., Gong, X., Wang, Y., Zhang, Y., Tang, Y., Zhou, X., Liu, H., Huang, Y., Zhang, J., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315550121 · Cited by 17
“…for the selective autophagy of invading pathogens (xenophagy) (15–17), Nix, FUNDC1 for the selective autophagy of mitochondria (mitophagy) (18, 19), FAM134B, Sec62, CCPG1, RTN3, TEX264, ATL3 for the selective autophagy of endoplasmic reticulum (ER - phagy) (20–26), STBD1 for the selective…”
The role of mitophagy in the development of chronic kidney disease
Yang, K., Li, T., Geng, Y., Zou, X., Peng, F., & Gao, W. (2024) · PeerJ · doi:10.7717/peerj.17260 · Cited by 16
“It recruits autophagosomes to mitochondria by directly binding to ATG8-family proteins ( Novak et al., 2010 ).”
Mitochondrial Regulation by PINK1-Parkin Signaling
Imai, Y. (2012) · ISRN Cell Biology · doi:10.5402/2012/926160 · Cited by 15
Physiological Functions of Mitochondrial Reactive Oxygen Species
Choi, T. G., & Kim, S. S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.88386 · Cited by 22
“It directly recognizes autophagosome-sited GABA receptor-associated protein (GABARAP) that is a functional homolog of LC3 and subsequently induces mitophagy [126, 146].”
BackgroundReceptor-mediated mitophagy: a new target of neurodegenerative diseases
Yang, J., Yang, F., Chen, G., Liu, M., Yuan, S., & Zhang, T. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1665315 · Cited by 16
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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