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 accessAbstract
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.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“For example, blocking proteasome function may activate autophagy [610, 1017-1020], although those studies did not assess long-lived protein degradation.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [1020]
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 [131]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[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-citationTight 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
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
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,728
Research works printed but not linked: 1
- Lee, 1995, Am. J. Pathol., 147, 1811
Cited by
Sorted by citations
Items 701–800 of 809
Proximity interactome of LC3B in normal growth conditionsPreprint
Nollet, M., Agrotis, A., Michailidis, F., Dokal, A. D., Rajeeve, V., Burden, J. J., Nightingale, T. D., Cutillas, P. R., Ketteler, R., & Kermorgant, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.08.463639 · Cited by 1
Qiu, B., Zhong, Z., Dou, L., Xu, Y., Zou, Y., Weldon, K. S., Wang, J., Zhang, L., Liu, M., Williams, K. E., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2679397/v1 · Cited by 1
Neddylation Regulates Mitochondrial Dynamics and Turnover in the Adult HeartPreprint
Zou, J., Wang, W., Chen, Q., Zhang, L., Zambrano-Carrasco, J., Li, Y., Lu, Y., Zhou, H., Dong, K., Fukai, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.03.692150 · Cited by 1
Excess Met1-ubiquitination leads to solid aggregate formationPreprint
Kaypee, S., Miyasaka, M., NAKAJIMA, T., Nishimura, H., Sakamaki, J.-I., Komatsu, M., & Ikeda, F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.20.700516 · Cited by 1
Self-citationRegulation of the p62 promoter by oxidative damage in neurodegenerative disease and aging
Du, Y. (2009) · Cited by 1
Manley, S. (2014) · KU ScholarWorks (The University of Kansas)
XBP1, Unfolded Protein Response, and Endocrine Responsiveness
Clarke, R. C. (2009) · doi:10.21236/ada516632
Mechanism of Cargo Recognition During Selective Autophagy
Watanabe, Y., & Nobuo, N. (2012) · InTech eBooks · doi:10.5772/33894
Autophagy and antigen processing : strategies to enhance T cell recognition of cancer cells
Williams, L. (2014) · University of Birmingham Institutional Research Archive (University of Birmingham)
Liu, X. (2012) · UKnowledge (University of Kentucky)
Mechanisms Underlying the Cellular Clearance of Antitrypsin Z
Gelling, C. L., & Brodsky, J. L. (2012) · Proceedings of the American Thoracic Society
The Functions of Autophagy Genes in Lymphocytes and Osteoclasts
Miller, B. C. (2011) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7m043dz
Salmenperä, P. (2012) · Työväentutkimus Vuosikirja
P R O T E I N FA M I LY R E V I E W
Shpilka, T., Weidberg, H., Pietrokovski, S., & Elazar, Z. (2011)
REGULATION OF CARDIAC AUTOPHAGY IN RESPONSE TO LIPID OVERLOAD
Jaishy, B. P. (2013)
Defining the role of folliculin and its interacting partners
Seifan, S. (2016) · ORCA Online Research @Cardiff (Cardiff University)
The role of autophagy in clearance of protein aggregates
Isakson, P. (2011) · NORA - Norwegian Open Research Archives
CROSS-TALK BETWEEN THE UBIQUITIN-PROTEASOME SYSTEM AND MACROAUTOPHAGY
Pankiv, S., & Johansen, T. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0003
AUTOPHAGY IN AMYOTROPHIC LATERAL SCLEROSIS
Gál, J., & Zhu, H. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0009
Venkatesh, A. (2016) · eScholarship@UMassChan · doi:10.13028/m2nc7g
Interactions of L. monocytogenes with Host Cellular Defenses
Lam, G. Y. (2012) · TSpace (University of Toronto)
Examining the Role of Endoplasmic Reticulum Stress in Pancreatic Beta-cell Biology
Teodoro, T. (2012) · TSpace (University of Toronto)
Targeting Selective Autophagy of Insoluble Protein Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00005-9
Analysis of autophagy in lung cancer
Al‐Ali, R. (2016) · Gredos (University of Salamanca) · doi:10.14201/gredos.132790
Tao, L. (2018) · Springer eBooks · doi:10.1007/978-3-319-77495-4_5
C9orf72 expansions disrupt ATM-mediated DNA repair
Walker, C. (2018) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)
Programmed cell death mechanisms and nanoparticle toxicity
Madkour, L. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-822481-6.00010-4
Exploring selective autophagy in Drosophila: Methods to identify Atg8-interacting proteins
Petridi, S., Jacomin, A., Bhujabal, Z., Johansen, T., & Nezis, I. P. (2020) · Methods in cell biology · doi:10.1016/bs.mcb.2020.10.008
Development of new tools to study lipidated mammalian ATG8Preprint
Park, S., Jeon, P., Yamasaki, A., Lee, H., Mun, J. Y., Jun, Y., Park, J.-H., Lee, S.-H., Lee, S.-K., Song, H. K., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-221701/v1
Self-citationThe role of autophagy in Alzheimer disease
Jaeger, P. A. (2011) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-8320
Noda, N. N., & Inagaki, F. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-405877-4.00002-0
Busse, R. A. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3900
Lipton, S. A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727653084.793538935
Jenny, A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732071110.793538790
GMAP is an Atg8a-Interacting Protein that Regulates Golgi Turnover In DrosophilaPreprint
Rahman, M. A., Lőrincz, P., Juhász, G., Zhang, Y., & Nezis, I. P. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3920639
Diehl, J. A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.725967101.793538077
Inhibition of Autophagy by a Small Molecule through Covalent Modification of the LC3 Protein
Fan, S., Yue, L., Wan, W., Zhang, Y., Zhang, B., Otomo, C., Li, Q., Lin, T., Hu, J., Xu, P., et al. (2021) · Angewandte Chemie · doi:10.1002/ange.202109464
Boggio, V. (2011) · doi:10.3998/panc.2010.10
Liu, Y., Trnka, M. J., He, L., Burlingame, A. L., & Correia, M. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.13.512146
Wnt5a-Ror2 signaling activates p62-Nrf2 axis in reactive astrocytes after brain injuryPreprint
Endo, M., Tanaka, Y., Fukuoka, M., Suzuki, H., & Minami, Y. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.19.537450
ATG8 family protein, cargo selection, and autophagy
Mishra, A., & Dhiman, R. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-90142-0.00006-2
Xin, C. A. I., Gao, J., Yan, Z., Zhang, H., Zhang, S., & Guo, D. (2023) · Research Square · doi:10.21203/rs.3.rs-3416817/v1
Machine learning approaches for the identification of ligands of the autophagy marker LC3
Soulère, L., & Queneau, Y. (2023) · Artificial Intelligence Chemistry · doi:10.1016/j.aichem.2023.100022
Beckers, J., Tharkeshwar, A. K., Fumagalli, L., Contardo, M., Schoor, E. V., Fazal, R., Thal, D. R., Chandran, S., Mancuso, R., Bosch, L. V. D., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24159426
Beckers, J., Tharkeshwar, A. K., Fumagalli, L., Contardo, M., Schoor, E. V., Fazal, R., Thal, D. R., Chandran, S., Mancuso, R., Bosch, L. V. D., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24159423
SAP30, a novel autophagy regulatory gene in neuroblastoma
Pathania, A. S., Murugan, A., Zahid, A., Chava, H., Coulter, D. W., Călin, G. A., & Challagundla, K. B. (2024) · Molecular Therapy Oncology · doi:10.1016/j.omton.2024.200916
Saha, S., Kumar, R. V., Sarangi, S., Gope, A., Pal, A., Tapader, R., Nag, N., & Pal, A. (2025) · Research Square · doi:10.1101/2025.01.11.632575
Maiti, S., Chedere, A., Jolly, M. K., Chandra, N. R., & Rangarajan, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.09.658583
Autophagy Receptors Couple Cargo Destined to Be Degraded with the Core Autophagy Machinery
Olsvik, H. L., Lamark, T., & Johansen, T. (2025) · Learning materials in biosciences · doi:10.1007/978-3-031-88121-3_4
Jiang, L., Wang, F., Huai, M., Zhang, W., Chen, X., Li, C., Zhang, X., Liu, B., Su, Y., Chu, M., et al. (2025) · Toxicology Letters · doi:10.1016/j.toxlet.2025.111744
Beckers, J., Tharkeshwar, A. K., Fumagalli, L., Contardo, M., Schoor, E. V., Fazal, R., Thal, D. R., Chandran, S., Mancuso, R., Bosch, L. V. D., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24159420
Yan, R.-L., Luan, C.-L., Liao, C.-C., Liu, L.-H., Chen, F.-Y., Chen, H.-Y., & Chen, R.-H. (2022) · Figshare · doi:10.6084/m9.figshare.19746434
Gao, M., Du, Z., Dong, Q., Su, S., & Tian, L. (2024) · Figshare · doi:10.6084/m9.figshare.26618821
Gao, M., Du, Z., Dong, Q., Su, S., & Tian, L. (2024) · Figshare · doi:10.6084/m9.figshare.26618827
Traver, M. K. (2013) · DukeSpace (Duke University)
Qiu, B., Zhong, Z., Dou, L., Xu, Y., Zou, Y., Weldon, K., Wang, J., Zhang, L., Liu, M., Williams, K. E., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26659447
Qiu, B., Zhong, Z., Dou, L., Xu, Y., Zou, Y., Weldon, K., Wang, J., Zhang, L., Liu, M., Williams, K. E., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26659444
Gao, M., Du, Z., Dong, Q., Su, S., & Tian, L. (2024) · Figshare · doi:10.6084/m9.figshare.26618824
p62/SQSTM1 selectively supports starvation-induced autophagy in N2a neuroblastoma cellsPreprint
Marimuthu, A., Saha, D., Vengataraghavan, V., Jivin, B. M. M., & Devanathan, V. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.03.697476
Mondal, P., Cyril, A., Mamriev, D., Parham, L. R., Wierzbicki, I. H., Shen, C., Doglioni, G., Dufrense, S., Komarla, A., Gonzalez, D. J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.03.703609
Legionella Lem26 functions as an ATG8-activated effector that inhibits host autophagy
Parducho, K. R., Yang, Z., Guinn, E. J., Choi, D., Nag, S., Melia, T. J., & Roy, C. R. (2026) · mBio · doi:10.1128/mbio.03595-25
A novel lipid-triggered allosteric site modulates LC3-LIR receptor binding activityPreprint
Gahlot, D., Jesu Castin, E., Mathur, S. C., Das, D., Kumar, A., Arun, A., Gain, C., Sharma, M., Pal, R. K., Jain, N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.10.710726
Yakut, S., Akı, R. H., & Mutluay, D. (2026) · Journal of Advances in VetBio Science and Techniques · doi:10.31797/vetbio.1860946
Coulon, P.-G. A. (2014) · theses.fr (ABES) · doi:10.70675/35505ce2z6226z4be3z9fc3za30de5ecacdc
Regulation of proteotoxicity through atypical NEDDylation
Maghames, C. M. (2016) · theses.fr (ABES) · doi:10.70675/f67a0612z3cccz46b5zb058zebfbc60f1ac4
Alfaisal, J. (2016) · theses.fr (ABES) · doi:10.70675/912b4531z9f61z4aacz89bez526a9131ecb9
Rôles de l’autophagie dans l'homéostasie des cellules souches intestinales
Trentesaux, C. (2018) · theses.fr (ABES) · doi:10.70675/6bad110bz19b1z4cd6z81d0z74d0fb1e27f3
Mechanisms and function of mitophagy in adaptation to heat stress during development of C. elegans
Chen, Y. (2019) · theses.fr (ABES) · doi:10.70675/c8145e7bz8153z43acz8532z3ea5954dd01c
Modulation de l'autophagie neuronale par la sérine protéase tPA en conditions ischémiques
Thiebaut, A. M. (2019) · theses.fr (ABES) · doi:10.70675/6586c0abz9e4cz455fz95ffzc52ec76397f8
Rôle de l’autophagie dans l’ostéosarcome
Camuzard, O. (2019) · theses.fr (ABES) · doi:10.70675/db9b0551zd9a2z4cf6z8dc4zdfbbe6b4e208
Lopez-Reyes, R. G. (2020) · theses.fr (ABES) · doi:10.70675/0cf3c9baz63d4z4ebfzb6efza0a5f5a241b2
de Calbiac, H. (2019) · theses.fr (ABES) · doi:10.70675/bafe951fz8332z4b0azb55bzac8a4af1955b
Mokhles, F., Azimee, S., Cordani, M., Rahmati, M., Fard, N. A., Djavaheri‐Mergny, M., & Moosavi, M. A. (2026) · Cell Death · doi:10.1016/j.celld.2026.100011
Kusunoki, H., Tanaka, T., Mizukami, T., Wakamatsu, K., & Nagata, T. (2026) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2026.141149
Wu, L., Gao, T., Ke, D., & 刘国明 (2026) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2025-0028
Wang, Y., Zhen, S., Sun, M., Su, L., & Yan, S. (2026) · Neurogastroenterology & Motility · doi:10.1111/nmo.70341
Lu, Y., Wang, N., Liu, M., Lu, Z., Fan, S., Lv, W., Lu, Y., Han, F., & Li, X. (2026) · Autophagy · doi:10.1080/15548627.2026.2674717
Saha, S., Kumar, R., Sarangi, S., Gope, A., Pal, A., Tapader, R., Nag, N., Bhattacharya, S., & Pal, A. (2026) · Molecular Medicine · doi:10.1186/s10020-026-01514-4
Lin, Y., Lai, Y.-H., Pang, J.-Y., Lin, Y., Chang, T., Fang, I., Wang, R.-H., Chang, C., Chiang, I., Wu, S., et al. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.202505913
Programmable Nanobody‐Targeting Chimeras Enable Intracellular Viral Protein Degradation
Pan, M. Y.-C., Lee, T.-H., Peng, T., Wu, E. Y.-H., Chiu, Y., Chiu, C.-C., Nguyễn, H. V., Pao, Y.-S., Chao, M., Lee, R. K., et al. (2026) · Advanced Science · doi:10.1002/advs.76687
Wang, L., Wang, X., Li, H., Ma, Y., Seeberger, P. H., Jing Hua, H. U., & Yin, J. (2026) · Small · doi:10.1002/smll.74938
A programmable lipid-triggered allosteric site modulates LC3 LIR receptor binding activity
Gahlot, D., Jesu Castin, E., Mathur, S. C., Das, D., Kumar, A., Arun, A., Gain, C., Sharma, M., Pal, R. K., Jain, N., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76697-9
Tuğrul, B., Alp, M., Irani, M., & Balcan, E. (2026) · Tissue and Cell · doi:10.1016/j.tice.2026.103902
Metadata
- 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
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-08
- Volume
- 283
- Issue
- 33
- Pages
- 22847-22857
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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