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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.
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“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]
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“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]
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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
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