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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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Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
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
Autophagosome formation: core machinery and adaptations
Xie, Z., & Klionsky, D. J. (2007) · Nature Cell Biology · doi:10.1038/ncb1007-1102 · Cited by 2,237
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124
Dynamics and diversity in autophagy mechanisms: lessons from yeast
Nakatogawa, H., Suzuki, K., Kamada, Y., & Ohsumi, Y. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2708 · Cited by 1,761
Selective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558
Bellot, G., Garcia-Medina, R., Gounon, P., Chiche, J., Roux, D., Pouysségur, J., & Mazure, N. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-09 · Cited by 1,501
A Role for Ubiquitin in Selective Autophagy
Kirkin, V., McEwan, D. G., Novak, I., & Đikić, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,268
Essential role for Nix in autophagic maturation of erythroid cells
Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185
A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates
Kirkin, V., Lamark, T., Sou, Y.-S., Bjørkøy, G., Nunn, J. L., Bruun, J.-A., Shvets, E., McEwan, D. G., Clausen, T. H., Wild, P., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.020 · Cited by 1,065
Cited by
Sorted by citations
Items 501–600 of 1,000
Mitochondrial biogenesis and fragmentation as regulators of protein degradation in striated muscles
Romanello, V., & Sandri, M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.08.001 · Cited by 70
“Bnip3L preferentially interacts with GABARAP whereas LC3 binds to the LIR motif in Bnip3 homodimers [72,73].”
BackgroundStructure biology of selective autophagy receptors
Kim, B.-W., Kwon, D. H., & Song, H. K. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.2.265 · Cited by 71
“selective autophagy is further divided into several sub-groups depending on its cargos: degradation of aggregated proteins (aggrephagy) (21-24), mitochondria (mitophagy) (25-32), per-”
BackgroundRegulation of Exercise-Induced Autophagy in Skeletal Muscle
Rocchi, A., & He, C. (2017) · Current Pathobiology Reports · doi:10.1007/s40139-017-0135-9 · Cited by 69
Mitophagy and Its Contribution to Metabolic and Aging-Associated Disorders
Liu, L., Liao, X., Wu, H., Li, Y., Zhu, Y., & Chen, Q. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.8013 · Cited by 69
“Further studies have indicated that NIX may be a mitophagy receptor that interacts with LC3 by an LIR motif and recruits LC3 to injured mitochondria to initiate mitophagy (153).”
Mitophagy Receptors in Tumor Biology
Xie, Y., Liu, J., Kang, R., & Tang, D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.594203 · Cited by 70
“In addition, BNIP3 has a tumor suppressor effect in pancreatic cancer (Okami et al., 2004), colorectal cancer (Murai et al., 2005; Bacon et al., 2007), and gastric cancer (Murai et al., 2005), which is related to hypermethylation of the BNIP3 promoter.”
BackgroundRole of Selective Autophagy in Spermatogenesis and Male Fertility
Lv, C., Wang, X., Guo, Y., & Yuan, S. (2020) · Cells · doi:10.3390/cells9112523 · Cited by 73
“Among them, NIX and BNIP3 interact with LC3 through their BH3 domain, further inducing mitophagy [23,24], while FUNDC1 directly binds to LC3 to induce mitochondrial autophagy under hypoxic conditions [25].”
BackgroundMechanism of Mitophagy and Its Role in Sepsis Induced Organ Dysfunction: A Review
Zhu, C., Yao, R.-Q., Li, L.-X., Li, P., Xie, J., Wang, J., & Deng, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.664896 · Cited by 75
“No positive result was obtained in clinical trials regarding TNF-α (anti-tumor necrosis factor-α) antibodies, highdose steroids, and activated protein C (Nunnally, 2016).”
BackgroundIriondo, M. N., Etxaniz, A., Varela, Y. R., Ballesteros, U., Lázaro, M., Valle, M., Fracchiolla, D., Martens, S., Montes, L. R., Goñi, F. M., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04704-z · Cited by 73
“Although the cell can recognize the cargo to be degraded independently of LC3/GABARAP [18–20], in certain types of selective autophagy, LC3/GABARAP proteins are able to participate in cargo selection, interacting with different receptors [21, 22], which can be proteins[23, 24] or lipids [25–28].”
BackgroundFBXL4 ubiquitin ligase deficiency promotes mitophagy by elevating NIX levels
Elcocks, H., Brazel, A. J., McCarron, K. R., Kaulich, M., Husnjak, K., Mortiboys, H., Clague, M. J., & Urbé, S. (2023) · The EMBO Journal · doi:10.15252/embj.2022112799 · Cited by 64
“In distinction to mitophagy adaptors utilized by the PINK1 – Parkin pathway, BNIP3 and NIX integrate into the outer mitochondrial membrane and then recruit the phagophore membrane via their LIR motifs, in common with other selective autophagy adaptors (Novak et al , 2010; Hanna et al , 2012).”
BNIP3 is degraded by ULK1-dependent autophagy via MTORC1 and AMPK
Park, C. W., Hong, S. M., Kim, E., Kwon, J. H., Kim, K., Nam, H. G., & Choi, K. Y. (2013) · Autophagy · doi:10.4161/auto.23072 · Cited by 69
“BNIP3 contains several defined domains such as the PEST domain (amino acids 54 to 81), a BH3 domain (amino acids 104 to 119) and a transmembrane domain (TM, amino acids 164 to 184), MAP1LC3-interacting region (LIR, amino acids 18 to 21).(11,12) Because the promoter of BNIP3 contains a hypoxia response element (HRE) an…”
BackgroundMitophagy in hematopoietic stem cells
Joshi, A., & Kundu, M. (2013) · Autophagy · doi:10.4161/auto.26681 · Cited by 72
Nix: A receptor protein for mitophagy in mammals
Kanki, T. (2010) · Autophagy · doi:10.4161/auto.6.3.11420 · Cited by 69
A Mechanistic Review of Mitophagy and Its Role in Protection against Alcoholic Liver Disease
Williams, J. A. R., & Ding, W. (2015) · Biomolecules · doi:10.3390/biom5042619 · Cited by 68
“The autophagy receptor proteins then further recruit autophagosomes likely via directly interacting with the LC3 protein to selectively envelop the receptor decorated mitochondria and eventually transport the damaged mitochondria to lysosomes for their degradation.”
BackgroundInfluentialSwerdlow, N., & Wilkins, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249661 · Cited by 66
“(FUNDC1), Nip3-like protein X (NIX); and IMM proteins cardiolipin and prohibitin 2 (PHB2) are the most studied receptors which mediate mitophagy [14,43,59-64].”
BackgroundThe Emerging Roles of Autophagy in Human Diseases
Lei, Y., & Klionsky, D. J. (2021) · Biomedicines · doi:10.3390/biomedicines9111651 · Cited by 68
“Besides; some OMM proteins such as BNIP3L and FUNDC1 can themselves function as the receptor [29,30].”
BackgroundChemotherapy Resistance: Role of Mitochondrial and Autophagic Components
Bahar, E., Han, S., Kim, J., & Yoon, H. (2022) · Cancers · doi:10.3390/cancers14061462 · Cited by 67
Sancho, A., Durán, J., García‐España, A., Mauvezin, C., Alemu, E. A., Lamark, T., Macías, M. J., DeSalle, R., Royo, M., Sala, D., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034034 · Cited by 72
“Thus, DOR gene family products add to the growing list of proteins, such as p62, NBR1 or NIX, that bind to LC3/GABARAP proteins through an LIR motif [20,21,30,31,32,37].”
BackgroundAutophagy as a Regulatory Component of Erythropoiesis
Zhang, J., Wu, K., Xiao, X., Liao, J., Hu, Q., Chen, H., Liu, J., & An, X. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16024083 · Cited by 70
“Nix is also a selective receptor that combines with mammalian Atg8 homologs, including microtubule-associated protein light chain 3 (LC3/GABARAP) and ubiquitin-like modifiers, which are indispensable for the maturation of phagophores and autophagosomes [22].”
BackgroundAutophagy Contributes to the Quality Control of Leaf Mitochondria
Nakamura, S., Hagihara, S., Otomo, K., Ishida, H., Hidema, J., Nemoto, T., & Izumi, M. (2020) · Plant and Cell Physiology · doi:10.1093/pcp/pcaa162 · Cited by 69
“…B-cell lymphoma 2 (BCL2) family members, BCL2/adenovirus E1B 19 kDa-interacting protein 3 (BNIP3), BNIP3L/Nix and Bcl2like 13 (Bcl2L13) also bridge mitochondria and mammalian ATG8 homologs to induce mitophagy (Schweers et al. 2007, Sandoval et al. 2008, Novak et al. 2010, Murakawa et al. 2015).”
BackgroundHIF1α-dependent mitophagy facilitates cardiomyoblast differentiation
Zhao, J.-F., Rodger, C. E., Allen, G. F. G., Weidlich, S., & Ganley, I. G. (2020) · Cell Stress · doi:10.15698/cst2020.05.220 · Cited by 61
“served LC3-interacting regions (LIRs) [23-27].”
Paez, H. G., Pitzer, C. R., & Alway, S. E. (2023) · Cells · doi:10.3390/cells12020249 · Cited by 71
“Up n mitochondrial localization, Parkin is ctivated and decorates OMM proteins with olyubiquitin chains [187] (Figure 3), thereby promoting mitophagy through interacti ns with autophagy a apter pr teins [188,189].”
Reggiori, F., Komatsu, M., Finley, K. D., & Simonsen, A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/156272 · Cited by 68
“Nix/Bnip3L, an autophagy receptor whose structure resembles that of Atg32, is also an outer mitochondrial membrane protein that interacts with GABARAP [170, 171] and plays an important role in mitophagy during erythroid differentiation [172, 173] (Figure 3(c)).”
BackgroundBudzik, J. M., Swaney, D. L., Jimenez‐Morales, D., Johnson, J. R., Garelis, N. E., Repasy, T., Roberts, A. W., Popov, L. M., Parry, T. J., Pratt, D. R., et al. (2020) · eLife · doi:10.7554/elife.51461 · Cited by 62
The fluorescence toolbox for visualizing autophagy
Ding, S., & Hong, Y. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00913j · Cited by 63
Müller, M., Kötter, P., Behrendt, C., Walter, E., Scheckhuber, C. Q., Entian, K.-D., & Reichert, A. S. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.044 · Cited by 67
Diversity of mitophagy pathways at a glance
Ganley, I. G., & Simonsen, A. (2022) · Journal of Cell Science · doi:10.1242/jcs.259748 · Cited by 67
Autophagic Clearance of Mitochondria in the Kidney Copes with Metabolic Acidosis
Namba‐Hamano, T., Takabatake, Y., Kimura, T., Takahashi, A., Yamamoto, T., Matsuda, J., Kitamura, H., Niimura, F., Matsusaka, T., Iwatani, H., et al. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013090986 · Cited by 66
Mitophagy in atherosclerosis: from mechanism to therapy
Zhang, Y., Weng, J., Huan, L., Sheng, S., & Xu, F. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1165507 · Cited by 67
“Studies have demonstrated (98) that BNIP3L is a mitophagy receptor that may bind LC3 via the LIR motif at its N-terminus.”
BackgroundAutophagy and cancer cell metabolism
Anderson, C. M., & Macleod, K. F. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.06.002 · Cited by 63
“NIX (or BNIP3L) is also a HIF1 target and both BNIP3 and NIX appear to function analogously to promote mitophagy through interaction with LC3B-II/GABARAP via a conserved LIR motif in their amino termini (Hanna et al., 2012; Novak et al., 2010; Schwarten et al., 2009).”
BackgroundThe Aging Heart: Mitophagy at the Center of Rejuvenation
Liang, W., & Gustafsson, Å. B. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.00018 · Cited by 65
Elorza, Á. A., & Soffia, J. P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.625020 · Cited by 64
“NIX protein is highly expressed in erythroid precursors and is needed for erythropoiesis (Novak et al., 2009).”
BackgroundPINK1, Keap1, and Rtnl1 regulate selective clearance of endoplasmic reticulum during development
Wang, R., Fortier, T. M., Chai, F., Miao, G., Shen, J. L., Restrepo, L. J., Digiacomo, J. J., Velentzas, P. D., & Baehrecke, E. H. (2023) · Cell · doi:10.1016/j.cell.2023.08.008 · Cited by 63
The lifecycle of skeletal muscle mitochondria in obesity
Pileggi, C. A., Parmar, G., & Harper, M. (2021) · Obesity Reviews · doi:10.1111/obr.13164 · Cited by 61
Autophagy, reactive oxygen species and the fate of mammalian cells
Szumiel, I. (2010) · Free Radical Research · doi:10.3109/10715762.2010.525233 · Cited by 61
Cheng, H., Gang, X., Liu, Y., Wang, G., Zhao, X., & Wang, G. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00179.2019 · Cited by 63
The role of autophagy in bacterial infections
Castrejón-Jiménez, N. S., Leyva-Paredes, K., Hernández-González, J. C., Luna‐Herrera, J., & García‐Pérez, B. E. (2015) · BioScience Trends · doi:10.5582/bst.2015.01035 · Cited by 62
“This type of autophagy can be classified according to the substrate degraded: protein aggregates (aggrephagy) (27,28); peroxisomes (pexophagy) (19,29); mitochondria (mitophagy) (18,30); glycogen (glycophagy) (31); endoplasmic reticulum (reticulophagy) (15); zymogen granules (zymophagy) (32); lipids (lipophagy) (20); r…”
BackgroundPINK1 and Parkin regulate IP3R-mediated ER calcium release
Ham, S. J., Yoo, H., Woo, D., Lee, D. H., Park, K., & Chung, J. (2023) · Nature Communications · doi:10.1038/s41467-023-40929-z · Cited by 67
“At the mitochondria, Nix functions as a selective autophagy receptor, facilitating the recruitment of LC3B 71 .”
BackgroundBetin, V. M. S., MacVicar, T., Parsons, S. F., Anstee, D. J., & Lane, J. D. (2012) · Autophagy · doi:10.4161/auto.19227 · Cited by 60
“During erythropoiesis, mitochondria are targeted for mitophagy by the actions of Nix(24)—an adaptor for Atg8 family members.(22) Intriguingly, mitochondria that persist in Nix mice that are deficient in erythroid mitophagy retain high membrane potential,(19,25) meanwhile the requirement for Nix during erythroid mitoph…”
BackgroundMitochondria get a Parkin' ticket
Wild, P. S., & Đikić, I. (2010) · Nature Cell Biology · doi:10.1038/ncb0210-104 · Cited by 60
Mitochondrial functions and rare diseases
Dard, L., Blanchard, W., Hubert, C., Lacombe, D., & Rossignol, R. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100842 · Cited by 65
The Dawn of Mitophagy: What Do We Know by Now?
Belousov, D. M., Вячеславовна, М. Е., Somasundaram, S. G., Kirkland, C. E., & Aliev, G. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200522202319 · Cited by 60
“By contrast to BNIP3, NIX recruits to mitochondrial membrane gamma-aminobutyric acid receptorassociated protein-like 1 (GABARAP-L1) upon stress conditions [186].”
BackgroundInfluentialMitophagy in aging and longevity
Guo, J., & Chiang, W. (2021) · IUBMB Life · doi:10.1002/iub.2585 · Cited by 60
Thomas, R. L., & Gustafsson, Å. B. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-0835 · Cited by 58
Alternative Macroautophagic Pathways
Juenemann, K., & Reits, E. A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/189794 · Cited by 58
Hamacher‐Brady, A., Choe, S., Locker, J. K., & Brady, N. R. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.101 · Cited by 58
“MitoGFP/RFP, GFP-LC3B, GFP-GATE-16, WT and DLIR mCherry-Nix and mCherryBnip3 were as described previously.(16,17) In text and figure legends, tagRFP and mCherry are both referred to as RFP.”
MethodAutophagy: A necessary event during erythropoiesis
Grosso, R. A., Fader, C. M., & Colombo, M. I. (2017) · Blood Reviews · doi:10.1016/j.blre.2017.04.001 · Cited by 63
Mitochondria orchestrate macrophage effector functions in atherosclerosis
Dumont, A., Lee, M., Barouillet, T., Murphy, A. J., & Yvan‐Charvet, L. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100922 · Cited by 60
Monitoring Mitophagy in Neuronal Cell Cultures
Zhu, J., Dagda, R. K., & Chu, C. T. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-328-8_21 · Cited by 59
“Nix, a BH3-only member of the Bcl-2 family, is a mitochondrial outer membrane protein that is essential for autophagic elimination of mitochondria during red blood cell development (16).”
BackgroundWu, H., Wei, H., Sehgal, S. A., Liu, L., & Chen, Q. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.030 · Cited by 58
Springer, M. Z., Poole, L. P., Drake, L. E., Bock-Hughes, A., Boland, M. L., Smith, A. G., Hart, J. A. L., Chourasia, A. H., Liu, I. Z., Bozek, G., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1877469 · Cited by 61
The Roles of Mitochondrial Dysfunction and Reactive Oxygen Species in Aging and Senescence
Zia, A., Farkhondeh, T., Pourbagher‐Shahri, A. M., & Samarghandian, S. (2021) · Current Molecular Medicine · doi:10.2174/1566524021666210218112616 · Cited by 70
Role of autophagy in β ‐cell function and mass
Hur, K. Y., Jung, H. S., & Lee, M. ‐. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01278.x · Cited by 58
Naoi, M., Maruyama, W., & Shamoto‐Nagai, M. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02150-w · Cited by 58
Nix-Mediated Mitophagy Modulates Mitochondrial Damage During Intestinal Inflammation
Vincent, G., Novak, E. A., Siow, V. S., Cunningham, K. E., Griffith, B. D., Comerford, T. E., Mentrup, H. L., Stolz, D. B., Loughran, P., Ranganathan, S., et al. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7702 · Cited by 60
“NIX has been shown to contain an LC3-interacting region in its cytoplasmic domain, which allows for direct binding of the two proteins (38, 41).”
BackgroundNovel Insights into the Anti-Aging Role of Mitophagy
(2018) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2018.05.005 · Cited by 56
Autophagy Signaling in Skeletal Muscle of Infarcted Rats
Jannig, P. R., Moreira, J. B. N., Bechara, L. R. G., Bozi, L. H. M., Bacurau, A. V. N., Monteiro, A. W. A., Dourado, P. M. M., Wisløff, U., & Brum, P. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085820 · Cited by 56
“Specifically, upregulation of Fis1 protein triggers mitochondrial fission, an important step preceding mitophagy [42], while Bnip3 is a crucial protein involved in mitophagy process [43].”
BackgroundIanniciello, A., Zarou, M. M., Rattigan, K. M., Scott, M. T., Dawson, A., Dunn, K. M., Brabcová, Z., Kalkman, E. R., Nixon, C., Michie, A. M., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd5016 · Cited by 55
Wu, N., Zheng, W., Zhou, Y., Tian, Y., Tang, M., Feng, X., Ashrafizadeh, M., Wang, Y. Z., Niu, X., Tambuwala, M. M., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102428 · Cited by 59
Jiang, L., Hara‐Kuge, S., Yamashita, S., & Fujiki, Y. (2014) · Genes to Cells · doi:10.1111/gtc.12198 · Cited by 56
Manifestations of Age on Autophagy, Mitophagy and Lysosomes in Skeletal Muscle
Triolo, M., & Hood, D. A. (2021) · Cells · doi:10.3390/cells10051054 · Cited by 60
Garrido‐Maraver, J., Paz, M. V., Cordero, M. D., Lorite, J. B., Oropesa-Ávila, M., de la Mata, M., Pavón, A. D., de Lavera, I., Alcocer‐Gómez, E., Galán, F., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.027 · Cited by 58
Zhang, W., Chen, C., Wang, J., Liu, L., He, Y., & Chen, Q. (2018) · Physiology · doi:10.1152/physiol.00030.2017 · Cited by 56
“(LC3-interacting region) motif and are able to recruit ATG8 proteins (LC3 and its homolog GABARAP, gamma-aminobutyric acid receptor-associated protein) to mitochondria to activate mitophagy (6, 56, 64, 91, 92, 101, 107, 109, 117, 139, 155).”
BackgroundInfluentialMitophagy: A crucial modulator in the pathogenesis of chronic diseases
Yang, X., Pan, W., Xu, G., & Chen, L. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.008 · Cited by 55
Mitophagy Regulates Neurodegenerative Diseases
Cen, X., Zhang, M., Zhou, M., Ye, L., & Xia, H. (2021) · Cells · doi:10.3390/cells10081876 · Cited by 60
“Studies show that NIX binds to LC3/GABARAP via its LIR motif located at its N-terminal, thereby causing autophagosomal membrane formation [40].”
BackgroundQin, X., Wang, R., Xu, H., Tu, L., Chen, H., Li, H., Liu, N., Wang, J., Li, S., Yin, F., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.2022360 · Cited by 55
The role of autophagic degradation in the heart
Nishida, K., Taneike, M., & Otsu, K. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.029 · Cited by 53
Selective Autophagy by Close Encounters of the Ubiquitin Kind
Vainshtein, A., & Grumati, P. (2020) · Cells · doi:10.3390/cells9112349 · Cited by 59
Choe, S. C., Hamacher‐Brady, A., & Brady, N. R. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0115-9 · Cited by 55
“Moreover, the autophagy receptor Bnip3L/ Nix, a close homologue of Bnip3 [13], and Bcl-xL are coupregulated during red blood cell (RBC) maturation [54].”
BackgroundBeyond starvation: An update on the autophagic machinery and its functions
Kawabata, T., & Yoshimori, T. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.12.005 · Cited by 56
An inter‐species protein–protein interaction network across vast evolutionary distance
Zhong, Q., Pevzner, S. J., Hao, T., Wang, Y., Mosca, R., Menche, J., Taipale, M., Taşan, M., Fan, C., Yang, X., et al. (2016) · Molecular Systems Biology · doi:10.15252/msb.20156484 · Cited by 54
“Two of the six human interactors (BNIP3L, TBC1D5) are known to interact with the human homologs of Atg8 (Rual et al, 2005; Novak et al, 2010; Popovic et al, 2012; Rolland et al, 2014).”
Tol, M. J., Ottenhoff, R., van Eijk, M., Zelcer, N., Aten, J., Houten, S. M., Geerts, D., van Roomen, C. P. A. A., Bierlaagh, M. C., Scheij, S. S., et al. (2016) · Diabetes · doi:10.2337/db16-0243 · Cited by 54
Liang, C., Gao, Y., He, Y., Han, Y., Manthari, R. K., Tikka, C., Chen, C., Wang, J., & Zhang, J. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.113438 · Cited by 53
Yu, W., Liao, J., Yang, F., Zhang, H., Chang, X., Yang, Y., Bilal, R. M., Wei, G., Liang, W., Guo, J., et al. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.111968 · Cited by 54
Lipids and Lipid-Binding Proteins in Selective Autophagy
de la Ballina, L. R., Munson, M. J., & Simonsen, A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.051 · Cited by 54
The Role of Mitophagy in Skeletal Muscle Damage and Regeneration
Chatzinikita, E., Maridaki, M. D., Palikaras, K., Koutsilieris, M., & Philippou, Α. (2023) · Cells · doi:10.3390/cells12050716 · Cited by 63
“Specifically, phosphorylation of FUNDC1 at Ser13 and Tyr18 reduces its activity [74,84], while its phosphorylation at Ser17 by ULK1 increases FUNDC1 interaction [75].”
BackgroundNix interacts with WIPI2 to induce mitophagy
Bunker, E. N., Guerroué, F. L., Wang, C., Strub, M., Werner, A. A., Tjandra, N., & Youle, R. J. (2023) · The EMBO Journal · doi:10.15252/embj.2023113491 · Cited by 57
“We found that LIR point mutations significantly blocked mitophagy induced by Nix as previously reported (Novak et al , 2010; Ordureau et al , 2021), but not as substantially as the L75A mutation (Fig 7A and B).”
InfluentialStaying young at heart: autophagy and adaptation to cardiac aging
Leon, L. J., & Gustafsson, Å. B. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.11.006 · Cited by 53
Activating Autophagy as a Therapeutic Strategy for Parkinson’s Disease
Fowler, A. J., & Moussa, C. (2018) · CNS Drugs · doi:10.1007/s40263-018-0497-5 · Cited by 51
Molecular mechanisms and clinical implications of multiple forms of mitophagy in the heart
Saito, T., Hamano, K., & Sadoshima, J. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa340 · Cited by 50
“agy, Bnip3- and Nix-mediated mechanisms play a significant role in mediating reticulocyte differentiation.(18,19) Besides the aforementioned ubiquitin-dependent mitophagy and receptor-dependent mitophagy, recent evidence suggests that Ulk1-/”
Nix/BNIP3L‐dependent mitophagy accounts for airway epithelial cell injury induced by cigarette smoke
Zhang, M., Shi, R., Zhang, Y., Hu, S., Zhang, Q., Yang, X., Li, Y., & Zhang, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28117 · Cited by 51
“Nix (also known as BNIP3L) is a member of the BH3‐only subfamily of Bcl2 family protein and involved in mitophagy and cell death (Novak et al., 2010).”
BackgroundChoi, C., Vo, M. T., Nicholas, J., & Choi, Y. B. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00868-y · Cited by 51
Gang, H., Hai, Y., Dhingra, R., Gordon, J. W., Yurkova, N., Aviv, Y., Li, H., Aguilar, F., Marshall, A. J., Leygue, E., et al. (2011) · Circulation Research · doi:10.1161/circresaha.110.238709 · Cited by 54
The receptor proteins: pivotal roles in selective autophagy
Xu, Z., Yang, L., Xu, S., Zhang, Z., & Cao, Y. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv055 · Cited by 57
“However, mutation of the LRS domain has a partial effect on NIX-mediated mitochondrial clearance in vivo, indicating that other properties of NIX also participate in this progress [18].”
BackgroundHass, D. T., & Barnstable, C. J. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.2702-18.2019 · Cited by 51
Nix-mediated mitophagy regulates platelet activation and life span
Zhang, W., Ma, Q., Siraj, S., Ney, P. A., Liu, J., Liao, X., Yuan, Y., Li, W., Liu, L., & Chen, Q. (2019) · Blood Advances · doi:10.1182/bloodadvances.2019032334 · Cited by 52
“Loss of Nix leads to mitochondrial retention in erythrocytes, defective erythroid maturation, and anemia.(14,32,33,36-38) Because both platelets and red blood cells are anucleates from the same hematopoietic cell lineage,(39) we were interested to investigate whether Nix plays a role in mediating mitophagy in platelet…”
BackgroundInfluentialMitochondrial Dynamics Imbalance: A Strategy for Promoting Viral Infection
Ren, Z., Zhang, X., Ding, T., Zhong, Z., Hu, H., Xu, Z., & Deng, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01992 · Cited by 50
Xu, K., Lu, C., Ren, X., Wang, J., Xu, P., & Zhang, Y. (2021) · Environmental Toxicology · doi:10.1002/tox.23327 · Cited by 51
Autophagy and mitophagy interplay in melanoma progression
Maes, H., & Agostinis, P. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.07.003 · Cited by 50
“NIX also functions as a LIR-containing mitochondrial receptor [63-65] and can contribute to mitochondrial priming by”
BackgroundMitophagy: Basic Mechanism and Potential Role in Kidney Diseases
Tang, C., He, L., Liu, J., & Dong, Z. (2015) · Kidney Diseases · doi:10.1159/000381510 · Cited by 51
Mitophagy and neurodegeneration
Wager, K., & Russell, C. (2013) · Autophagy · doi:10.4161/auto.25082 · Cited by 51
Pathophysiological Role of Autophagy: Lesson from Autophagy-Deficient Mouse Models
Ichimura, Y., & Komatsu, M. (2011) · EXPERIMENTAL ANIMALS · doi:10.1538/expanim.60.329 · Cited by 50
“tion with Atg8p/LC3 family proteins [77, 78].”
BackgroundThe Physiological Role of Mitophagy: New Insights into Phosphorylation Events
Hirota, Y., Kang, D., & Kanki, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/354914 · Cited by 50
“Nix, in both in vivo and in vitro assays, interacts with LC3/GABARAP, which anchors to the isolation membrane and is involved in isolation membrane extension, and this Nix-LC3/GABARAP interaction is thought to mediate efficient targeting of mitochondria to autophagosomes [66, 67].”
BackgroundTcf19 is a novel islet factor necessary for proliferation and survival in the INS-1 β-cell line
Krautkramer, K. A., Linnemann, A. K., Fontaine, D. A., Whillock, A. L., Harris, T. W., Schleis, G. J., Truchan, N. A., Marty‐Santos, L., Lavine, J. A., Cleaver, O. B., et al. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00147.2013 · Cited by 50
Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?
Khalil, B., & Liévens, J.-C. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.211179 · Cited by 51
Assessment of Autophagy in Neurons and Brain Tissue
Benito‐Cuesta, I., Díez, H., Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2017) · Cells · doi:10.3390/cells6030025 · Cited by 52
“However, it must be taken into account that certain types of mitophagy induced by BNIP3L/NIX are dependent on gamma-aminobutyric acid receptor-associated protein (GABARAP) and they are less dependent on LC3 proteins [39,40].”
BackgroundPUMA dependent mitophagy by Abrus agglutinin contributes to apoptosis through ceramide generation
Panda, P. K., Naik, P. P., Meher, B. R., Das, D. N., Mukhopadhyay, S., Praharaj, P. P., Maiti, T. K., & Bhutia, S. K. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.12.002 · Cited by 50
“For example, Nix induces mitophagy in order to eliminate mitochondria during the late phase of erythrocyte maturation [6].”
BackgroundTherapeutic Modulation of Autophagy in Leukaemia and Lymphoma
Djavaheri‐Mergny, M., Giuriato, S., Tschan, M. P., & Humbert, M. (2019) · Cells · doi:10.3390/cells8020103 · Cited by 52
“Selective autophagy can also occur through an ubiquitin–independent mechanism wherein autophagy adaptors such NIX and FAM134B bind directly to mitochondria and the endoplasmic reticulum (ER), respectively [11,12].”
BackgroundValionyte, E., Yang, Y., Roberts, S. L., Kelly, J., Lu, B., & Luo, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.11.012 · Cited by 51
Gurubaran, I. S., Viiri, J., Koskela, A. K. J., Hyttinen, J. M. T., Paterno, J. J., Kis, G. N., Antal, M., Urtti, A. O., Kauppinen, A., Felszeghy, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061976 · Cited by 52
“The second group of mitophagy receptors [20] contains a transmembrane domain that can directly bind to the OMM and stimulate autophagosome formation via their LIR motifs, namely Bnip3 (BCL2 interacting protein 3) [71], Nix/Bnip3L (BCL2-like 3) [72], FUNDC1 (FUN14 domain containing 1) [73] and Bcl2L13 (BCL2-like 13) [7…”
BackgroundCastets, P., Frank, S., Sinnreich, M., & Rüegg, M. A. (2016) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-160153 · Cited by 49
“It involves specific receptors, such as Bnip3, that are able to interact with depolarized mitochondria and the autophagic machinery [110, 111].”
Background
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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