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

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Structural Basis for Sorting Mechanism of p62 in Selective Autophagy

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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

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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.

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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

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Structural Basis for Sorting Mechanism of p62 in Selective Autophagy

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