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p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
Open accessAbstract
Protein degradation by basal constitutive autophagy is important to avoid accumulation of polyubiquitinated protein aggregates and development of neurodegenerative diseases. The polyubiquitin-binding protein p62/SQSTM1 is degraded by autophagy. It is found in cellular inclusion bodies together with polyubiquitinated proteins and in cytosolic protein aggregates that accumulate in various chronic, toxic, and degenerative diseases. Here we show for the first time a direct interaction between p62 and the autophagic effector proteins LC3A and -B and the related gamma-aminobutyrate receptor-associated protein and gamma-aminobutyrate receptor-associated-like proteins. The binding is mediated by a 22-residue sequence of p62 containing an evolutionarily conserved motif. To monitor the autophagic sequestration of p62- and LC3-positive bodies, we developed a novel pH-sensitive fluorescent tag consisting of a tandem fusion of the red, acid-insensitive mCherry and the acid-sensitive green fluorescent proteins. This approach revealed that p62- and LC3-positive bodies are degraded in autolysosomes. Strikingly, even rather large p62-positive inclusion bodies (2 microm diameter) become degraded by autophagy. The specific interaction between p62 and LC3, requiring the motif we have mapped, is instrumental in mediating autophagic degradation of the p62-positive bodies. We also demonstrate that the previously reported aggresome-like induced structures containing ubiquitinated proteins in cytosolic bodies are dependent on p62 for their formation. In fact, p62 bodies and these structures are indistinguishable. Taken together, our results clearly suggest that p62 is required both for the formation and the degradation of polyubiquitin-containing bodies by autophagy.
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“This fluorescent reporter is designed to monitor LC3 flux through the autophagy pathway because the GFP signal is sensitive to the acidic and/or proteolytic conditions of the lysosome lumen, whereas mCherry fluorescence persists under these environments.4, 17”
From Measurement of autophagy flux in the nervous system in vivo (2013) · cites this paper as [17]
In the citing paper
“Nutritional starvation suppresses TORC1-mediated Atg1 phosphorylation [423,509] while stimulating Atg1mediated Atg13 phosphorylation [586, 744, 745].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [423]
In the citing paper
“Lys48-linked polyubiquitin chains are a signal for proteasome-dependent degradation, while Lys63-linked polyubiquitin chains play other roles, such as regulating autophagy-dependent cargo recognition by interacting with the scaffold protein p62 (also known as SQSTM1)40.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [40]
In the citing paper
“SQSTM1 mutations affecting the UBA domain impair ubiquitin recognition [130], whereas mutations within the LIR domain impact LC3 recognition and substrate delivery to the autophagosomes [84,131].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [84]
Citations
Cites
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N. G., Palmer, A. E., & Tsien, R. Y. (2004) · Nature Biotechnology · doi:10.1038/nbt1037 · Cited by 4,619
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
Self-citationTowards a proteome-scale map of the human protein–protein interaction network
Rual, J.-F. M., Venkatesan, K., Hao, T., Hirozane-Kishikawa, T., Dricot, A., Li, N., Berriz, G. F., Gibbons, F. D., Dreze, M., Ayivi-Guedehoussou, N., et al. (2005) · Nature · doi:10.1038/nature04209 · Cited by 2,904
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
A guide to choosing fluorescent proteins
Shaner, N. C., Steinbach, P. A., & Tsien, R. Y. (2005) · Nature Methods · doi:10.1038/nmeth819 · Cited by 2,823
A Human Protein-Protein Interaction Network: A Resource for Annotating the Proteome
Stelzl, U., Worm, U., Lalowski, M. M., Haenig, C., Brembeck, F. H., Goehler, H., Strödicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.029 · Cited by 2,433
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Items 101–200 of 1,039
Pankiv, S., Alemu, E. A., Brech, A., Bruun, J., Lamark, T., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200907015 · Cited by 684
Self-citationAutophagy mediates degradation of nuclear lamina
Dou, Z., Xu, C., Donahue, G., Shimi, T., Pan, J.-A., Zhu, J., Ivanov, A., Capell, B. C., Drake, A. M., Shah, P. P., et al. (2015) · Nature · doi:10.1038/nature15548 · Cited by 655
Self-citationLC3/GABARAP family proteins: autophagy‐(un)related functions
Schaaf, M. B. E., Keulers, T. G., Vooijs, M., & Rouschop, K. M. A. (2016) · The FASEB Journal · doi:10.1096/fj.201600698r · Cited by 665
Nguyen, T. N., Padman, B. S., Usher, J., Oorschot, V., Ramm, G., & Lazarou, M. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201607039 · Cited by 668
Selective autophagy: ubiquitin-mediated recognition and beyond
Kraft, C., Peter, M., & Hofmann, K. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-836 · Cited by 639
A Sensitive and Quantitative Technique for Detecting Autophagic Events Based on Lysosomal Delivery
Katayama, H., Kogure, T., Mizushima, N., Yoshimori, T., & Miyawaki, A. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.05.013 · Cited by 650
Autophagy: The Master of Bulk and Selective Recycling
Marshall, R. S., & Vierstra, R. D. (2018) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042817-040606 · Cited by 621
Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702115 · Cited by 626
Self-citationPersistent activation of Nrf2 through p62 in hepatocellular carcinoma cells
Inami, Y., Waguri, S., Sakamoto, A., Kouno, T., Nakada, K., Hino, O., Watanabe, S., Ando, J., Iwadate, M., Yamamoto, M. P., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201102031 · Cited by 615
Mechanisms of Selective Autophagy
Zaffagnini, G., & Martens, S. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.004 · Cited by 636
Spatial Coupling of mTOR and Autophagy Augments Secretory Phenotypes
Narita, M., Young, A. R. J., Arakawa, S., Samarajiwa, S. A., Nakashima, T., Yoshida, S., Hong, S., Berry, L. S., Reichelt, S., Ferreira, M., et al. (2011) · Science · doi:10.1126/science.1205407 · Cited by 594
Immune activation in brain aging and neurodegeneration: too much or too little?
Lucin, K. M., & Wyss-Coray, T. (2009) · Neuron · doi:10.1016/j.neuron.2009.08.039 · Cited by 679
Jin, Z., Li, Y., Pitti, R. M., Lawrence, D. A., Pham, V. C., Lill, J. R., & Ashkenazi, A. (2009) · Cell · doi:10.1016/j.cell.2009.03.015 · Cited by 588
The ubiquitin ligase parkin mediates resistance to intracellular pathogens
Manzanillo, P. S., Ayres, J. S., Watson, R. O., Collins, A. C., Souza, G., Rae, C. S., Schneider, D. S., Nakamura, K., Shiloh, M. U., & Cox, J. S. (2013) · Nature · doi:10.1038/nature12566 · Cited by 588
The Adaptor Protein p62/SQSTM1 Targets Invading Bacteria to the Autophagy Pathway
Zheng, Y. T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T., & Brumell, J. H. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900441 · Cited by 616
Self-citationBacteria–autophagy interplay: a battle for survival
Huang, J., & Brumell, J. H. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3160 · Cited by 590
Mechanisms of cross‐talk between the ubiquitin‐proteasome and autophagy‐lysosome systems
Korolchuk, V. I., Menzies, F. M., & Rubinsztein, D. C. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.047 · Cited by 581
Lysosome-mediated processing of chromatin in senescence
Ivanov, A., Pawlikowski, J., Manoharan, I., van Tuyn, J., Nelson, D. M., Rai, T. S., Shah, P. P., Hewitt, G., Korolchuk, V. I., Passos, J. F., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201212110 · Cited by 539
Cleaning house: selective autophagy of organelles
Anding, A. L., & Baehrecke, E. H. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.016 · Cited by 576
Synthetic lethal metabolic targeting of cellular senescence in cancer therapy
Dörr, J. R., Yu, Y., Milanovic, M., Beuster, G., Zasada, C., Däbritz, J. H. M., Lisec, J., Lenze, D., Gerhardt, A., Schleicher, K., et al. (2013) · Nature · doi:10.1038/nature12437 · Cited by 541
Autophagy Protects against Sindbis Virus Infection of the Central Nervous System
Orvedahl, A., MacPherson, S., Sumpter, R., Tallóczy, Z., Zou, Z., & Levine, B. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.01.007 · Cited by 558
Atg8‐family interacting motif crucial for selective autophagy
Noda, N. N., Ohsumi, Y., & Inagaki, F. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.018 · Cited by 553
Endoplasmic Reticulum and the Unfolded Protein Response
Bravo, R., Parra, V., Gatica, D., Rodriguez, A. E., Torrealba, N., Paredes, F., Wang, Z. V., Antonio Zorzano, A., Hill, J. A., Jaimovich, E., et al. (2013) · International review of cytology · doi:10.1016/b978-0-12-407704-1.00005-1 · Cited by 575
Atg8: an autophagy-related ubiquitin-like protein family.
Shpilka, T., Weidberg, H., Pietrokovski, S., & Elazar, Z. (2011) · Genome biology · doi:10.1186/gb-2011-12-7-226 · Cited by 543
“The motif in p62 responsible for binding Atg8, the LC3interacting region (LIR, also known as Atg8-interacting motif, AIM) [104,105], is common to other proteins that interact with Atg8 proteins, including Nbr1 [106], Atg3 [107], Nix [96] and the yeast cytoplasm-to-vacuole targeting receptor Atg19 [108].”
BackgroundCancer Chemoprevention Mechanisms Mediated Through the Keap1–Nrf2 Pathway
Hayes, J. D., McMahon, M. J., Chowdhry, S., & Dinkova‐Kostova, A. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3221 · Cited by 549
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Clague, M. J., & Urbé, S. (2010) · Cell · doi:10.1016/j.cell.2010.11.012 · Cited by 535
Autophagy in thymic epithelium shapes the T-cell repertoire and is essential for tolerance
Nedjic, J., Aichinger, M., Emmerich, J., Mizushima, N., & Klein, L. (2008) · Nature · doi:10.1038/nature07208 · Cited by 552
Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
Kim, P. K., Hailey, D. W., Mullen, R. T., & Lippincott‐Schwartz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810611105 · Cited by 556
A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway
Kirkin, V., & Rogov, V. V. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.005 · Cited by 536
LC3- and p62-based biochemical methods for the analysis of autophagy progression in mammalian cells
Jiang, P., & Mizushima, N. (2014) · Methods · doi:10.1016/j.ymeth.2014.11.021 · Cited by 534
Leeman, D. S., Hebestreit, K., Ruetz, T., Webb, A. E., McKay, A., Pollina, E. A., Dulken, B. W., Zhao, X., Yeo, R. W., Ho, T. T., et al. (2018) · Science · doi:10.1126/science.aag3048 · Cited by 528
Murrow, L. M., & Debnath, J. (2012) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163918 · Cited by 546
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522
Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 545
Physiological significance of selective degradation of p62 by autophagy
Komatsu, M., & Ichimura, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.017 · Cited by 524
Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy
Poillet-Perez, L., Despouy, G., Delage-Mourroux, R., & Boyer-Guittaut, M. (2015) · Redox Biology · doi:10.1016/j.redox.2014.12.003 · Cited by 503
Matrix Protein 2 of Influenza A Virus Blocks Autophagosome Fusion with Lysosomes
Gannagé, M., Dormann, D., Albrecht, R., Dengjel, J., Torossi, T., Rämer, P. C., Lee, M., Strowig, T., Arrey, F., Conenello, G., et al. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.09.005 · Cited by 526
Cellular Strategies of Protein Quality ControlPreprint
Chen, B., Retzlaff, M., Roos, T. R., & Frydman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004374 · Cited by 515
p62 Is a Key Regulator of Nutrient Sensing in the mTORC1 Pathway
Duran, A., Amanchy, R., Linares, J. F., Joshi, J., Abu-Baker, S., Porollo, A., Hansen, M., Moscat, J., & Diaz-Meco, M. T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.038 · Cited by 472
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 514
Self-citationProtein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
Obesity, inflammation, and liver cancer
Sun, B., & Karin, M. (2011) · Journal of Hepatology · doi:10.1016/j.jhep.2011.09.020 · Cited by 507
Amm, I., Sommer, T., & Wolf, D. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 509
Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · Cited by 494
Autophagosome Formation and Molecular Mechanism of Autophagy
Tanida, I. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3482 · Cited by 505
Bae, S. H., Sung, S. H., Oh, S. Y., Lim, J. M., Lee, S. K., Park, Y. N., Lee, H. E., Kang, D., & Rhee, S. G. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.002 · Cited by 492
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Hill, B. G., Benavides, G. A., Lancaster, J. R., Ballinger, S. W., Dell’Italia, L., Zhang, J., & Darley-Usmar, V. M. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0198 · Cited by 495
Keap1 degradation by autophagy for the maintenance of redox homeostasis
Taguchi, K., Fujikawa, N., Komatsu, M., Ishii, T., Unno, M., Akaike, T., Motohashi, H., & Yamamoto, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121572109 · Cited by 482
The ATG conjugation systems in autophagy
Mizushima, N. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.12.001 · Cited by 483
Kubli, D. A., Zhang, X., Lee, Y., Hanna, R. A., Quinsay, M. N., Nguyen, C. K., Jimenez, R., Petrosyan, S., Murphy, A. N., & Gustafsson, Å. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.411363 · Cited by 476
SIRT1 is downregulated by autophagy in senescence and ageing
Xu, C., Wang, L., Fozouni, P., Evjen, G., Chandra, V., Jiang, J., Lu, C., Nicastri, M. C., Bretz, C. L., Winkler, J. D., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00579-5 · Cited by 478
Self-citationAutophagy: for better or for worse
Wirawan, E., Berghe, T. V., Lippens, S., Agostinis, P., & Vandenabeele, P. (2011) · Cell Research · doi:10.1038/cr.2011.152 · Cited by 485
Biogenesis and Cargo Selectivity of Autophagosomes
Weidberg, H., Shvets, E., & Elazar, Z. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052709-094552 · Cited by 466
The Role of Autophagy in Parkinson's DiseasePreprint
Lynch-Day, M. A., Mao, K., Wang, K., Zhao, M., & Klionsky, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009357 · Cited by 477
HMGB1 release and redox regulates autophagy and apoptosis in cancer cells
Tang, D., Kang, R., Cheh, C.-W., Livesey, K. M., Liang, X., Schapiro, N. E., Benschop, R., Sparvero, L. J., Amoscato, A. A., Tracey, K. J., et al. (2010) · Oncogene · doi:10.1038/onc.2010.261 · Cited by 461
Stingele, S., Stoehr, G., Peplowska, K., Cox, J., Mann, M., & Storchova, Z. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.40 · Cited by 468
Lou, G., Palikaras, K., Lautrup, S., Scheibye‐Knudsen, M., Tavernarakis, N., & Fang, E. F. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.07.002 · Cited by 455
Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451
Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437
Listeria monocytogenes ActA-mediated escape from autophagic recognition
Yoshikawa, Y., Ogawa, M., Hain, T., Yoshida, M., Fukumatsu, M., Kim, M., Mimuro, H., Nakagawa, I., Yanagawa, T., Ishii, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1967 · Cited by 469
Control of autophagy as a therapy for neurodegenerative disease
Harris, H., & Rubinsztein, D. C. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.200 · Cited by 450
Smith, M. D., Harley, M. E., Kemp, A. J., Wills, J. C., Lee, M. W., Arends, M. J., von Kriegsheim, A., Behrends, C., & Wilkinson, S. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.11.024 · Cited by 452
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Liu, S., Pi, J., & Zhang, Q. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102389 · Cited by 471
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Leu, J. I.-J., Pimkina, J. S., Frank, A. K., Murphy, M. E., & George, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.023 · Cited by 451
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Filimonenko, M., Isakson, P., Finley, K. D., Anderson, M. R., Jeong, H., Melia, T. J., Bartlett, B. J., Myers, K. M., Birkeland, H. C. G., Lamark, T., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.007 · Cited by 449
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Xu, X., Araki, K., Li, S., Han, J., Ye, L., Tan, W. G., Konieczny, B. T., Bruinsma, M. W., Martinez, J., Pearce, E. L., et al. (2014) · Nature Immunology · doi:10.1038/ni.3025 · Cited by 438
Huntingtin functions as a scaffold for selective macroautophagy
Rui, Y.-N., Xu, Z., Patel, B., Chen, Z., Chen, D., Tito, A., David, G., Sun, Y., Stimming, E. F., Bellen, H. J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3101 · Cited by 423
Structural basis of target recognition by Atg8/LC3 during selective autophagy
Noda, N. N., Kumeta, H., Nakatogawa, H., Satoo, K., Adachi, W., Ishii, J., Fujioka, Y., Ohsumi, Y., & Inagaki, F. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01238.x · Cited by 437
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Liu, D., Wu, H., Wang, C., Li, Y., Tian, H., Siraj, S., Sehgal, S. A., Wang, X., Wang, J., Shang, Y., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0251-z · Cited by 439
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Lamark, T., & Johansen, T. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120219-035530 · Cited by 429
Self-citationMcafee, Q. W., Zhang, Z., Samanta, A., Levi, S. M., Ma, X.-H., Piao, S., Lynch, J. P., Uehara, T., Sepulveda, A. R., Davis, L. E., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118193109 · Cited by 430
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Bhujabal, Z., Birgisdottir, Å. B., Sjøttem, E., Brenne, H. B., Øvervatn, A., Habisov, S., Kirkin, V., Lamark, T., & Johansen, T. (2017) · EMBO Reports · doi:10.15252/embr.201643147 · Cited by 430
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Itakura, E., & Mizushima, N. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009067 · Cited by 430
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Halling, J. F., & Pilegaard, H. (2020) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2020-0005 · Cited by 430
The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy
Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404
Autophagy in lysosomal storage disorders
Lieberman, A. P., Puertollano, R., Raben, N., Slaugenhaupt, S., Walkley, S. U., & Ballabio, A. (2012) · Autophagy · doi:10.4161/auto.19469 · Cited by 399
Diverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376
p62/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
Wong, Y., & Holzbaur, E. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1870-13.2014 · Cited by 380
Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 410
Autophagy in acute kidney injury
Kaushal, G. P., & Shah, S. V. (2016) · Kidney International · doi:10.1016/j.kint.2015.11.021 · Cited by 389
Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation
Gao, C., Cao, W., Bao, L., Zuo, W., Xie, G., Cai, T., Fu, W., Zhang, J., Wu, W., Zhang, X., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2082 · Cited by 393
Mitochondrial quality control mechanisms as molecular targets in cardiac ageing
Picca, A., Mankowski, R. T., Burman, J. L., Donisi, L., Js, K., Marzetti, E., & Leeuwenburgh, C. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0059-z · Cited by 399
IFITM3 Inhibits Influenza A Virus Infection by Preventing Cytosolic Entry
Feeley, E. M., Sims, J. S., John, S. P., Chin, C. R., Pertel, T., Chen, L.-M., Gaiha, G. D., Ryan, B. J., Donis, R. O., Elledge, S. J., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002337 · Cited by 402
Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function
Jaber, N. L., Dou, Z., Chen, J., Catanzaro, J. M., Jiang, Y.-P., Ballou, L. M., Selinger, E. S., Ouyang, X., Lin, R. Z., Zhang, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112848109 · Cited by 399
TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
Longatti, A., Lamb, C. A., Razi, M., Yoshimura, S., Barr, F. A., & Tooze, S. A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201111079 · Cited by 392
Wang, I.-F., Guo, B.-S., Liu, Y.-C., Wu, C.-C., Yang, C.-H., Tsai, K.-J., & Shen, C.-K. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206362109 · Cited by 377
Autophagy: a multifaceted intracellular system for bulk and selective recycling
Li, F., & Vierstra, R. D. (2012) · Trends in Plant Science · doi:10.1016/j.tplants.2012.05.006 · Cited by 394
Nezis, I. P., Simonsen, A., Sagona, A. P., Finley, K., Gaumer, S., Contamine, D., Rusten, T. E., Stenmark, H., & Brech, A. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200711108 · Cited by 370
Self-citationRestoring polyamines protects from age-induced memory impairment in an autophagy-dependent manner
Gupta, V., Scheunemann, L., Eisenberg, T., Mertel, S., Bhukel, A., Koemans, T. S., Kramer, J. M., Liu, K. S. Y., Schroeder, S., Stunnenberg, H. G., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3512 · Cited by 376
Young, M. M., Takahashi, Y., Khan, O. A., Park, S., Hori, T., Yun, J. K., Sharma, A. K., Amin, S., Hu, C., Zhang, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309104 · Cited by 393
Copper is an essential regulator of the autophagic kinases ULK1/2 to drive lung adenocarcinoma
Tsang, T., Posimo, J. M., Gudiel, A. A., Cicchini, M., Feldser, D. M., & Brady, D. C. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0481-4 · Cited by 373
Sarkar, S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130134 · Cited by 380
Targeting Mitochondrial Dysfunction: Role for PINK1 and Parkin in Mitochondrial Quality Control
Narendra, D. P., & Youle, R. J. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3799 · Cited by 367
Sahani, M. H., Itakura, E., & Mizushima, N. (2014) · Autophagy · doi:10.4161/auto.27344 · Cited by 348
A current perspective of autophagosome biogenesis
Shibutani, S., & Yoshimori, T. (2013) · Cell Research · doi:10.1038/cr.2013.159 · Cited by 368
Metadata
- Authors
- Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T.
- Affiliations
- UiT The Arctic University of Norway (NO)
- Corresponding author
- Johansen, Terje
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 282
- Issue
- 33
- Pages
- 24131-24145
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2014918593
- Cited by
- 4,578
- References
- 55
- Citations by year
- 2026: 167 · 2025: 210 · 2024: 256 · 2023: 278 · 2022: 281 · 2021: 318 · 2020: 309 · 2019: 299 · 2018: 299 · 2017: 325 · 2016: 276 · 2015: 258 · 2014: 264 · 2013: 253 · 2012: 262
- FWCI
- 73.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- p62, LC3, autophagy, aggresomes, protein degradation, autolysosomes, neurodegenerative diseases, inclusion bodies
- MeSH terms
- Sequestosome-1 Protein, Amino Acid Sequence, Autophagy, Cytosol, Fluorescent Dyes, HeLa Cells, Humans, Microtubule-Associated Proteins, Protein Binding, Transfection, Ubiquitin, RNA, Small Interfering, Multiprotein Complexes, Adaptor Proteins, Signal Transducing
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