Cited by 4,578Autophagy in Disease and TherapyUbiquitin and proteasome pathwaysAmyotrophic Lateral Sclerosis Research

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p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

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Pankiv, Serhiy, Clausen, Terje Høyvarde, Lamark, Trond, Brech, Andreas, Bruun, Jack-Ansgar, Outzen, Heidi, Øvervatn, Aud, Bjørkøy, Geir, Johansen, Terje·2007·Journal of Biological Chemistry

DOI 10.1074/jbc.m702824200

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Abstract

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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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
ORCID: Pankiv, Serhiy
Lamark, Trond
Brech, Andreas
Bruun, Jack-Ansgar
Bjørkøy, Geir
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)
DOI: 10.1074/jbc.m702824200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4793 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, 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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p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

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