Cited by 809Autophagy in Disease and TherapyUbiquitin and proteasome pathwaysAmyotrophic Lateral Sclerosis Research

The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.

Structural Basis for Sorting Mechanism of p62 in Selective Autophagy

Open access

Ichimura, Yoshinobu, Kumanomidou, Taichi, Sou, Yu-shin, Mizushima, Tsunehiro, Ezaki, Junji, Ueno, Takashi, Kominami, Eiki, Yamane, Takashi, Tanaka, Keiji, Komatsu, Masaaki·2008·Journal of Biological Chemistry

DOI 10.1074/jbc.m802182200

Open this paper in CoChat — free account

Abstract

Impairment of autophagic degradation of the ubiquitin- and LC3-binding protein "p62" leads to the formation of cytoplasmic inclusion bodies. However, little is known about the sorting mechanism of p62 to autophagic degradation. Here we identified a motif of murine p62 consisting of 11 amino acids (Ser334-Ser344) containing conserved acidic and hydrophobic residues across species, as an LC3 recognition sequence (LRS). The crystal structure of the LC3-LRS complex at 1.56 angstroms resolution revealed interaction of Trp340 and Leu343 of p62 with different hydrophobic pockets on the ubiquitin fold of LC3. In vivo analyses demonstrated that p62 mutants lacking LC3 binding ability accumulated without entrapping into autophagosomes in the cytoplasm and subsequently formed ubiquitin-positive inclusion bodies as in autophagy-deficient cells. These results demonstrate that the intracellular level of p62 is tightly regulated by autophagy through the direct interaction of LC3 with p62 and reveal that selective turnover of p62 via autophagy controls inclusion body formation.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1074/jbc.m802182200

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
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
Self-citation
Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943
MOLREP : an Automated Program for Molecular Replacement
Vagin, A. A., & Teplyakov, A. (1997) · Journal of Applied Crystallography · doi:10.1107/s0021889897006766 · Cited by 4,756
p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
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
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
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
Development by Self-Digestion
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,728

Flagged first, then by citations

Show all 44 references

Research works printed but not linked: 1

Lee, 1995, Am. J. Pathol., 147, 1811

Sorted by citations

Items 601–700 of 809

TECPR1 provides E3-ligase like activity to the ATG5-ATG12 complex to conjugate LC3/ATG8 to damaged lysosomesPreprint
Wang, Y., Jefferson, M. A., Whelband, M., Kreuzer, K., McColl, J. T., Verkade, P., Mayer, U., & Wileman, T. E. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.24.546289 · Cited by 7
Compound Danshen Tablets ameliorate myocardial ischemia/reperfusion injury-induced ventricular remodeling by regulating autophagy via AMPK/mTOR signaling pathway
Li, Q., Luo, Y., Guo, H., Liu, W., Yu, H., Li, C., Chen, R., & Sun, X. (2024) · Chinese Herbal Medicines · doi:10.1016/j.chmed.2024.03.003 · Cited by 7
p62 and NBR1 functions are dispensable for aggrephagy in mouse ESCs and ESC-derived neurons
Trapannone, R., Romanov, J., & Martens, S. (2023) · Life Science Alliance · doi:10.26508/lsa.202301936 · Cited by 6
Activation of lysosomal degradative pathway in spinal cord tissues of carbon disulfide-treated rats
Gao, Y., Wang, S., Yi, A., Kou, R., Xie, K., & Song, F. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.05.016 · Cited by 7
Lipidation of BmAtg8 is required for autophagic degradation of p62 bodies containing ubiquitinated proteins in the silkworm, Bombyx mori
Ji, M.-M., Lee, J. M., Mon, H., Iiyama, K., Tatsuke, T., Morokuma, D., Hino, M., Yamashita, M., Hirata, K., & Kusakabe, T. (2017) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2017.08.006 · Cited by 7
SQSTM1L341V variant that is linked to sporadic ALS exhibits impaired association with MAP1LC3 in cultured cells
Nozaki, M., Otomo, A., Mitsui, S., Ono, S., Shirakawa, R., Chen, Y., Hama, Y., Sato, K., Chen, X., Suzuki, T., et al. (2020) · eNeurologicalSci · doi:10.1016/j.ensci.2020.100301 · Cited by 7
Identification of novel Atg3-Atg8 inhibitors using virtual screening for autophagy modulation
Leung, E. Y., Ayine‐Tora, D. M., Santos‐Ledo, A., Korolchuk, V. I., & Reynisson, J. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105092 · Cited by 7
The Role of Autophagy in Early Mammalian Embryonic Development
Tsukamoto, S., & Yamamoto, A. (2013) · Journal of Mammalian Ova Research · doi:10.1274/jmor.30.86 · Cited by 7
Toward effective Atg8‐based ATTECs: Approaches and perspectives
Schwalm, M. P., Knapp, S., & Rogov, V. V. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30380 · Cited by 6
Pathological study of progressive supranuclear palsy the cases with mutations in Bassoon
Wakita, M., Yaguchi, H., Otuski, M., Tanikawa, S., Miki, Y., Aiba, I., Yoshida, M., Nomura, T., Uwatoko, H., Mito, Y., et al. (2024) · Neuropathology · doi:10.1111/neup.13009 · Cited by 8
Ubiquitin-specific protease 7 exacerbates acute pancreatitis progression by enhancing ATF4-mediated autophagy
Peng, F., & Deng, X. (2025) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-024-01009-8 · Cited by 6
Total chemical synthesis of the phosphorylated p62 UBA domain reveals that Ser 407 Pi but not Ser 403 Pi enhances ubiquitin binding
Xu, L., Zhang, Y., Li, Y., & Lu, X. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob01906b · Cited by 7
In-Cell Chemical Crosslinking Identifies Hotspots for SQSTM-1/p62-IκBα Interaction That Underscore a Critical Role of p62 in Limiting NF-κB Activation Through IκBα Stabilization
Liu, Y., Trnka, M. J., He, L., Burlingame, A. L., & Correia, M. A. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100495 · Cited by 6
Autophagy regulates DNA repair by modulating histone ubiquitination
Wang, Y., Zhu, W., & Zhao, Y. (2016) · Molecular & Cellular Oncology · doi:10.1080/23723556.2016.1214772 · Cited by 6
Reduction of neuronal damage and promotion of locomotor recovery after spinal cord injury by early administration of methylprednisolone: possible involvement of autophagy pathway
Jin, Y., Yang, S., & Zhang, X. (2017) · RSC Advances · doi:10.1039/c6ra25794a · Cited by 5
Retracted
Chemical Biology of Autophagy-Related Proteins With Posttranslational Modifications: From Chemical Synthesis to Biological Applications
Luo, Y., Jiang, C., Yu, L., & Yang, A. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00233 · Cited by 8
In vitro reconstitution of autophagic processes
Alam, J. M., & Noda, N. N. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200130 · Cited by 6
AIM/LIR-based fluorescent sensors—new tools to monitor mAtg8 functions
Zientara‐Rytter, K., & Subramani, S. E. (2018) · Autophagy · doi:10.1080/15548627.2018.1454238 · Cited by 6
Pomolic acid and its glucopyranose ester promote apoptosis through autophagy in HT-29 colon cancer cells
Liu, L., Yu, T., Liao, T.-S., Xu, P., Wang, Y., Shi, M., & Li, B. (2023) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v15.i10.1756 · Cited by 5
Wnt5a/Ror2 promotes Nrf2‐mediated tissue protective function of astrocytes after brain injury
Endo, M., Tanaka, Y., Fukuoka, M., Suzuki, H., & Minami, Y. (2023) · Glia · doi:10.1002/glia.24483 · Cited by 5
The anticancer effects of pharmacological inhibition of autophagy in acute erythroid leukemia cells
Kazemi, A., Sadri, M., Houshmand, M., Yazdi, N., Zarif, M. N., Anjam-Najmedini, A., Tavakoli, R., Ojaghi, M., Ajami, M., Ajami, M., et al. (2018) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000000668 · Cited by 5
p62/Sequestosome 1 regulates transforming growth factor beta signaling and epithelial to mesenchymal transition in A549 cells
Trelford, C. B., Ng, E., Campbell, C. I., & Guglielmo, G. M. D. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110040 · Cited by 5
DAP1 regulates osteoblast autophagy via the ATG16L1–LC3 axis in Graves’ disease-induced osteoporosis
Gao, M., Du, Z., Dong, Q., Su, S., & Tian, L. (2023) · Journal of Orthopaedic Surgery and Research · doi:10.1186/s13018-023-04171-z · Cited by 5
Crosstalk between degradation and bioenergetics: how autophagy and endolysosomal processes regulate energy production
Pabon, A., Bhupana, J. N., & Wong, C. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-02095 · Cited by 6
Structure-Based Design and Discovery of a Potent and Cell-Active LC3A/B Covalent Inhibitor
Zhou, Z., Huang, S., Fan, S., Li, X., Wang, C., Yu, W., Du, D., Zhang, Y., Chen, K., Fu, W., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00898 · Cited by 5
Sequestosome 1/p62: a multi-domain protein with multi-faceted functions
Liu, X., Gál, J., & Zhu, H. (2012) · Frontiers in Biology · doi:10.1007/s11515-012-1217-z · Cited by 5
Visualization of reticulophagy in living cells using an endoplasmic reticulum-targeted p62 mutant
Wang, L., Liu, L., Qin, L., Luo, Q., & Zhang, Z. (2017) · Science China Life Sciences · doi:10.1007/s11427-015-9037-4 · Cited by 5
Analysis of microRNA expression profiles in exosomes derived from acute myeloid leukemia by p62 knockdown and effect on angiogenesis
Li, C., Long, X., Liang, P., Liu, Z., Wang, C., & Hu, R. (2022) · PeerJ · doi:10.7717/peerj.13498 · Cited by 5
Establishment of canine macrophages stably expressing GFP-tagged canine LC3 protein for effectively detecting autophagy
Cui, D., Huo, S., Wang, X., Zheng, Z., Zhang, Y., Zhang, J., & Zhong, F. (2019) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2019.101493 · Cited by 5
Membranous Structures Directly Come in Contact With p62/SQSTM1 Bodies
Tanida, I., Haruta, T., Suga, M., Takei, S., Takebe, A., Furuta, Y., Yamaguchi, J., Trejo, J. A. O., Kakuta, S., & Uchiyama, Y. (2021) · Journal of Histochemistry & Cytochemistry · doi:10.1369/00221554211011423 · Cited by 5
NBR1 directly promotes the formation of p62 – ubiquitin condensates via its PB1 and UBA domainsPreprint
Savova, A., Romanov, J., & Martens, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.18.303552 · Cited by 5
Correction: DOR/Tp53inp2 and Tp53inp1 Constitute a Metazoan Gene Family Encoding Dual Regulators of Autophagy and Transcription
Sancho, A., Durán, J., GarcÃa-EspaÃ±a, 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/annotation/f2e121d7-0878-44b1-a5c2-994231626fe1 · Cited by 5
Luminal B Breast Cancer Coexpressingp62andALDH1A3Is Less Susceptible to Radiotherapy
Ozaki, A., MATSUDA, A., Maemura, Y., Tada, Y., Kasai, T., Nagashima, Y., Onaga, C., Hara, Y., Kitabatake, K., Tsukimoto, M., et al. (2023) · Anticancer Research · doi:10.21873/anticanres.16786 · Cited by 4
Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins
Komatsu‐Hirota, S., Tabata, K., Sou, Y., Kakuta, S., Sakamaki, J.-I., Tsuchiya, H., Li, J., Kumeta, H., Sakai, Y., Fujioka, Y., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00785-1 · Cited by 4
Self-citation
N-Acetylneuraminic Acid Inhibits Melanogenesis via Induction of Autophagy
Yoshikawa, K., & Maeda, K. (2024) · Cosmetics · doi:10.3390/cosmetics11030082 · Cited by 4
Mechanism of mTOR/RILP-regulated autophagic flux in increased susceptibility to myocardial ischemia-reperfusion in diabetic mice
Zhao, J., Shi, W., Yan, Z., Wang, J., Yuan, M., Anwar, Y., He, Y., Ma, H., & Wu, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1506401 · Cited by 4
SQST-1/p62-regulated SKN-1/Nrf mediates a phagocytic stress response via transcriptional activation of lyst-1/LYST
Elkhalil, A., Whited, A., & Ghose, P. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011696 · Cited by 4
Sources of Oxidants and Function of ROS Inside the Macromolecule Cells
Madkour, L. H. (2020) · Nanomedicine and nanotoxicology · doi:10.1007/978-3-030-37297-2_3 · Cited by 4
Excluding the unwanted during autophagy
Sawa-Makarska, J. Z., & Martens, S. (2014) · Cell Cycle · doi:10.4161/cc.29826 · Cited by 4
Integrative analysis of Paneth cell proteomic and transcriptomic data from intestinal organoids reveals functional processes dependent on autophagyPreprint
Jones, E. J., Matthews, Z. J., Gul, L., Sudhakar, P., Treveil, A., Divekar, D., Buck, J., Wrzesinski, T., Jefferson, M., Armstrong, S. D., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/410027 · Cited by 4
Correction: DOR/Tp53inp2 and Tp53inp1 Constitute a Metazoan Gene Family Encoding Dual Regulators of Autophagy and Transcription
Sancho, A., Durán, J., GarcÃa-EspaÃ±a, 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/annotation/4d84cc19-b887-4c1e-a26f-1968819f8c70 · Cited by 4
Structural organization of p62 filaments and the cellular ultrastructure of calcium-rich p62-enwrapped lipid droplet cargoPreprint
Berkamp, S., Jungbluth, L., Katranidis, A., Mostafavi, S., Korculanin, O., Lu, P., Sharma, L., Thukral, L., Fitter, J., Dunin‐Borkowski, R. E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.15.618463 · Cited by 4
Schisandrin C Improves Chronic Stress-Induced Dyslipidemia in Mice by Regulating Pyroptosis and Autophagy Levels
Liu, Y., Lu, W., Huang, Y. M., Xu, C., Wu, W., Zhang, Z., Zhang, Y., Li, S., Wu, G., Wang, D., et al. (2025) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2501.01041 · Cited by 3
Chiral gold nanoparticles manipulate osteoimmune microenvironment via macrophage autophagy for bone regeneration
Wang, J., Gao, N., Wei, J., & Liao, L. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102131 · Cited by 3
TBK1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia: Mechanistic Insights into Impaired Autophagy and Proteostatic Failure
Manganelli, F., Perfetto, C., Carletta, O., & Gerbino, V. (2026) · Cells · doi:10.3390/cells15050477 · Cited by 4
Nuclear factor erythroid 2-related factor 2 in Alzheimer's disease
Murphy, K. E., & Park, J. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815868-5.00015-3 · Cited by 3
Role of autophagy in embryogenesis
Tatsumi, T., & Tsukamoto, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00020-6 · Cited by 3
Autophagy in chronic rhinosinusitis with or without nasal polyps
Pei, J., Ding, Z., Jiao, C., Tao, Y., Yang, H., & Li, J. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1417735 · Cited by 3
Choline kinase alpha regulates autophagy-associated exosome release to promote glioma cell progression
Li, J., Zhao, Y., Wu, X. R., Zou, Y., Liu, Y., & Ma, H. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.151269 · Cited by 3
Biological mechanisms of reactive oxygen species (ROS)
Madkour, L. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-822481-6.00002-5 · Cited by 3
Genetic ablation of p62/SQSTM1 demonstrates little effect on pancreatic β-cell function under autophagy deficiency
Fukae, T., Miyatsuka, T., Himuro, M., Wakabayashi, Y., Iida, H., Aoyama, S., Mita, T., Ikeda, F., Haruna, H., Takubo, N., et al. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.04.092 · Cited by 3
Salix babylonica L. mitigates pancreatic damage by regulating the Beclin-P62/SQSTM1 autophagy pathway in rats
Mahmoud, M. F., Tawfeek, N., Ali, N., Hasan, R. A., Sobeh, M., & El-Shazly, A. M. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116425 · Cited by 4
POU4F1 enhances lung cancer gemcitabine resistance by regulating METTL3-dependent TWF1 mRNA N6 adenosine methylation
Tang, J., Liu, Z., Xie, G., Wang, C., & Jiang, Y. (2024) · 3 Biotech · doi:10.1007/s13205-024-04161-w · Cited by 3
Advanced glycation end products induce autophagy in endothelial cells through oxidative stress and regulation of the RhoA-mTOR signaling pathway
Li, Y., Liang, F.-Q., Lin, S.-Z., Zeng, K., Cai, H.-D., & Liang, M. (2025) · Immunobiology · doi:10.1016/j.imbio.2025.153088 · Cited by 3
The study of freesia (Freesiaspp.) cut flowers quality in relation with nano silver in preservative solutions
Hajizadeh, H. S. (2016) · Acta Horticulturae · doi:10.17660/actahortic.2016.1131.1 · Cited by 3
Selective Autophagy
Rogov, V. V., & Kirkin, V. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-405877-4.00004-4 · Cited by 4
THE CELLULAR PROCESS OF AUTOPHAGY AND CONTROL OF AUTOPHAGY IN NEURONS
McKnight, N. C., Mizushima, N., & Yue, Z. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0001 · Cited by 3
GENETIC MOUSE MODELS FOR ELUCIDATION OF AUTOPHAGY-LYSOSOMAL SYSTEMS IN NEURONS UNDER PHYSIOLOGIC AND PATHOLOGIC CONDITIONS
Komatsu, M., Koike, M., Ichimura, Y., & Uchiyama, Y. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0008 · Cited by 3
Self-citation
Effects of the Rho GTPase ‐activating toxin CNF1 on fibroblasts derived from Rett syndrome patients: A pilot study
Cittadini, C., Germinario, E. A. P., Maroccia, Z., Cosentino, L., Maselli, V., Gambardella, L., Giambenedetti, M., Guidotti, M., Travaglione, S., Fallerini, C., et al. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17624 · Cited by 2
Autophagosomes coordinate an AKAP11-dependent regulatory checkpoint that shapes neuronal PKA signalingPreprint
Segura-Roman, A., Citron, Y. R., Shin, M., Sindoni, N., Maya-Romero, A., Rapp, S., Goul, C., Mancias, J. D., & Zoncu, R. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.06.606738 · Cited by 3
Peroxisomes as emerging clinical targets in neuroinflammatory diseases
Roczkowsky, A., Rachubinski, R. A., Hobman, T. C., & Power, C. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1642590 · Cited by 5
The oncogenic signalosome: SQSTM1/p62 as a master integrator of signaling, metabolism, and autophagy in cancer
Eun-ji, C., & Jeon, S.-M. (2026) · Toxicological Research · doi:10.1007/s43188-026-00349-9 · Cited by 7
Polyamines and autophagy as a dynamic regulatory network in skeletal muscle regeneration and aging
Attili, L., Rossi, M. N., Santo, R. D., Duranti, G., Ceci, R., & Cervelli, M. (2026) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2026.112188 · Cited by 3
miR-22a targets p62/SQSTM1 to negatively affect autophagy and disease resistance of grass carp (Ctenopharyngodon idella)
Yu, H., Xie, L., Chen, Z., Niu, H., Jia, X., Du, B., Shen, Y., Gui, L., Xu, X., & Li, J. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.109124 · Cited by 2
Methamphetamine-Induced Blood Pressure Sensitization Correlates with Morphological Alterations within A1/C1 Catecholamine Neurons
Busceti, C. L., Bucci, D., Damato, A., Lucia, M. D., Venturini, E., Ferrucci, M., Lazzeri, G., Puglisi‐Allegra, S., Scioli, M., Carrizzo, A., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910282 · Cited by 2
Liver CYP4A autophagic lysosomal degradation: A major role for the autophagic receptor SQSTM1/p62 through an uncommon target interaction site
He, L., Kwon, D., Trnka, M. J., Liu, Y., Yang, J., Li, K. H., Totah, R. A., Johnson, E. F., Burlingame, A. L., & Correia, M. A. (2025) · Molecular Pharmacology · doi:10.1016/j.molpha.2025.100061 · Cited by 2
Non-covalent SUMO interactions with ligases and effectors: SUMO-interacting motifs and beyond
Mishra, A., Cisse, E. H., & Suskiewicz, M. J. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253039 · Cited by 2
Cardiac Cytoarchitecture: How to Maintain a Working Heart—Waste Disposal and Recycling in Cardiomyocytes
Blondelle, J., & Lange, S. (2015) · Springer eBooks · doi:10.1007/978-3-319-15263-9_12 · Cited by 2
Molecular Machines Involved in Pexophagy
Nazarko, T. Y., & Farré, J. (2014) · Springer eBooks · doi:10.1007/978-3-7091-1788-0_22 · Cited by 2
Structural Studies of Mammalian Autophagy Lipidation Complex
Ohashi, K., Otomo, C., Metlagel, Z., & Otomo, T. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-8873-0_3 · Cited by 2
Marine-Derived Natural Product HDYL-GQQ-495 Targets P62 to Inhibit Autophagy
Li, Q., Fan, J., Chen, Y., Liu, Y., Liu, H., Jiang, W., Li, D., & Dang, Y. (2023) · Marine Drugs · doi:10.3390/md21020068 · Cited by 2
Biological functions and structural biology of Plasmodium falciparum autophagy‐related proteins: The under‐explored options for novel antimalarial drug design
Usman, M. A., Salman, A. A., Ibrahim, M. A., Furukawa, K., & Yamasaki, K. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14225 · Cited by 2
Autophagosome Formation
Karanasios, E., & Ktistakis, N. T. (2016) · Springer eBooks · doi:10.1007/978-3-319-33145-4_4 · Cited by 2
The interplay of SmNBR1 and SmATG8 in selective autophagy of the filamentous fungus Sordaria macrospora
Werner, A. (2018) · doi:10.53846/goediss-6798 · Cited by 1
LIR-dependent LMX1A/LMX1B autophagy crosstalk shapes human midbrain dopaminergic neuronal resiliencePreprint
Jiménez-Moreno, N., Stathakos, P., Antón, Z., Shoemark, D. K., Sessions, R. B., Witzgall, R., Caldwell, M. A., & Lane, J. D. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/636712 · Cited by 2
Inhibition of SQSTM1/p62 oligomerization and Keap1 sequestration by the Cullin-3 adaptor SHKBP1Preprint
Luan, L., Cao, X., & Baskin, J. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.21.634088 · Cited by 2
Mechanisms of Regulation of p62 in Autophagy and Implications for Health and Diseases
Takagi, K., & Mizushima, T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-405530-8.00002-9 · Cited by 1
Self-citation
Selective Disposal of Insoluble Protein Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00005-5 · Cited by 1
Unlocking the therapeutic promise of miRNAs in promoting amyloid-β clearance for Alzheimer's disease
Kaur, V., & Sunkaria, A. (2025) · Behavioural Brain Research · doi:10.1016/j.bbr.2025.115505 · Cited by 1
Dual inhibition of AKT and autophagy sensitizes triple negative breast cancer cells to carboplatin
Zhou, J.-Z., Wen, J.-Y., Xu, X., Zhao, N., Tang, J., Xiao, Y., Xiang, L., Jiang, Y., jiang, J.-W., Hong, H., et al. (2025) · Translational Oncology · doi:10.1016/j.tranon.2025.102434 · Cited by 2
P62/Sequestosome1 deficiency disrupts antioxidant and stress homeostasis during acute pancreatitis without exacerbating inflammation
Chen, W., Wang, J., Warabi, E., Imasaka, M., Takeda, Y., Nishiura, H., Takahashi, S., & Ohmuraya, M. (2025) · Pancreatology · doi:10.1016/j.pan.2025.07.416 · Cited by 1
Up-regulation of cell apoptosis, autophagy and mitochondrial dynamics in ovarian granulosa cells of Daurian ground squirrels during the pre-hibernation period
Wang, X., Li, H., Dong, Z., Lu, W., Chen, J., Zhang, H., Yuan, Z., Liu, Y., Weng, Q., & Han, Y. (2025) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2025.111927 · Cited by 1
The AP-4 accessory protein tepsin exhibits multivalent binding to LC3B
Cohen, C. I., Kendall, A. K., Wallace, N. S., McCorkle, M., & Jackson, L. P. (2025) · Advances in Biological Regulation · doi:10.1016/j.jbior.2025.101124 · Cited by 1
The application development of nanoparticle-based drug delivery systems in combating drug resistance of lung cancer
Li, D., Wang, X., Zhao, J., Shi, M., Chen, B., & Su, G. (2025) · Alexandria Engineering Journal · doi:10.1016/j.aej.2025.12.002 · Cited by 1
Cullin-3 adaptor SHKBP1 inhibits SQSTM1/p62 oligomerization and Keap1 sequestration
Luan, L., Cao, X., Xia, Z., Vaid, S., Leonetti, M. D., & Baskin, J. M. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202501207 · Cited by 3
Zika virus: unraveling the complex interplay between viral pathogenesis and host immune defenses
Zheng, S., Xiao, H., Suo, L., Luo, X., Mao, X., Li, Q., & Lin, X. (2026) · Virology Journal · doi:10.1186/s12985-026-03163-9 · Cited by 1
The Role of Cell Autophagy in Cancer and Its Application in Drug Discovery
Hong, M., Wang, N., & Feng, Y. (2015) · InTech eBooks · doi:10.5772/61780 · Cited by 1
Autophagy in Cystic Fibrosis Pathogenesis and Treatment
Cormet‐Boyaka, E., Caution, K., & Amer, A. O. (2016) · InTech eBooks · doi:10.5772/64686 · Cited by 1
Autophagy
Lewis, P. A., Pérez‐Carrión, M. D., & Piccoli, G. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803783-6.00006-7 · Cited by 2
COOH-terminal fragment of APP interacts with p62, forms an aggregate, and induces autophagic degradation in Alzheimer’s cell model
Tanaka, K., Kuramoto, K., Nakagawa, T., Nomura, Y., Ozawa, K., & Hosoi, T. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00003.2022 · Cited by 1
Self-citation
The participation of non-canonical autophagic proteins in the autophagy process and their potential as therapeutic targets
Yin, Y., Zhou, Y., Yang, X., Xu, Z., Yang, B., Luo, P., Yan, H., & He, Q. (2023) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2023.2177151 · Cited by 1
Enhanced autophagy and phagocytosis of apoptotic lymphocytes in splenic macrophages of acute ethanol-treated rats: Light and electron microscopic studies.
Betsuyaku, T., Ito, Y., Peake, N., Al‐Bari, M. A. A., El–Akabawy, G., & Eid, N. A. S. (2024) · PubMed · doi:10.14670/hh-18-729 · Cited by 1
Autophagy Accompanies Inflammasome Activation to Moderate Inflammation by Eliminating Active Inflammasomes
Nabar, N. R., Shi, C.-S., & Kehrl, J. H. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00016-0 · Cited by 1
Role of an autophagy/lysosome pathway in NF-κB pathway blocked pancreatic cancer Panc-1 cells.
Wu, T., Yang, Q., Chen, M., & Feng, Y. (2020) · PubMed Central · Cited by 1
Roles of phase separation and condensates in autophagy
Noda, N. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00021-x · Cited by 1
Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins
Rogov, V., SUZUKI, H., Marinkovi, M., Lang, V., Ryuichi, K. A. T. O., Kawasaki, M., Buljubai, M., prung, M., Rogova, N., Soichi Wakatsuki, A., et al. (2017) · Institutional Repositories DataBase (IRDB) · Cited by 1
Characterisation of the role of autophagy in DNA damage repair
Liu, E. Y. (2014) · Enlighten: Theses (The University of Glasgow) · Cited by 1
Examining Autophagy and Mitophagy as Inducible Mechanisms of Cellular Remodelling
Bloemberg, D. (2017) · UWSpace (University of Waterloo) · Cited by 1
Commentary: p62 plays a protective role in the autophagic degradation of polyglutamine protein oligomers in polyglutamine disease model flies
Nagai, Y. (2017) · Journal of Rare Diseases Research & Treatment · doi:10.29245/2572-9411/2017/3.1106 · Cited by 1
Atg8a interacts with transcription factor Sequoia to control the expression of autophagy genes in DrosophilaPreprint
Jacomin, A., Petridi, S., Monaco, M. D., Jain, A., Bhujabal, Z., Mulakkal, N. C., Palara, A., Powell, E. L., Chung, B., Zampronio, C. G., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/611731 · Cited by 1

Authors: Ichimura, Y., Kumanomidou, T., Sou, Y.-S., Mizushima, T., Ezaki, J., Ueno, T., Kominami, E., Yamane, T., Tanaka, K., & Komatsu, M.
Affiliations: Juntendo University (JP)
Nagoya University (JP)
Tokyo Metropolitan Institute of Medical Science (JP)
Corresponding author: Komatsu, Masaaki
ORCID: Ichimura, Yoshinobu
Sou, Yu-shin
Mizushima, Tsunehiro
Ueno, Takashi
Yamane, Takashi
Tanaka, Keiji
Komatsu, Masaaki
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2008-08
Volume: 283
Issue: 33
Pages: 22847-22857
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m802182200
OpenAlex: W2125123150
Semantic Scholar: 35145bb1648360bcd497256c99d185ca87c08d94
Cited by: 803
References: 44
Citations by year: 2026: 25 · 2025: 35 · 2024: 39 · 2023: 50 · 2022: 36 · 2021: 49 · 2020: 47 · 2019: 55 · 2018: 43 · 2017: 44 · 2016: 55 · 2015: 38 · 2014: 54 · 2013: 49 · 2012: 60
FWCI: 31.03
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4445 d)
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, selective autophagy, crystal structure, hydrophobic pocket, protein turnover
MeSH terms: Sequestosome-1 Protein, Autophagy, Binding Sites, Carrier Proteins, Lysosomes, Microtubule-Associated Proteins, Recombinant Fusion Proteins, Vacuoles, Sequence Deletion, Adaptor Proteins, Signal Transducing, Maltose-Binding Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structural Basis for Sorting Mechanism of p62 in Selective Autophagy

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks