ArticleNature communications2020
Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
72 citing papers in PubMed, 121 citations in OpenAlex.
- The role of E3 ubiquitin ligases in selective types of macroautophagy.EMBO reports · 2026Review
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- Functionalized Fluorescent Nanodiamonds Reveal Therapeutic Protein Clearance Through ENDOTAC Linked to AUTOTAC.Advanced healthcare materials · 2026Article
- A histidine switch controls the pH-responsive self-assembly of a helical protein filament.bioRxiv : the preprint server for biology · 2026Article
- Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins.The EMBO journal · 2026Article
- TBK1 Induces the Formation of Optineurin Filaments That Condensate with Polyubiquitin and LC3 for Cargo Sequestration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- SQSTM1/p62 UFMylation Enhances Autophagic Clearance of Pathogenic Mutant Huntingtin.International journal of biological sciences · 2026Article
- Therapeutic Promise of Mitophagy in Cancer: Advancing from Small-Molecule Regulation to Nanotechnology-Enhanced Targeting Therapy.Theranostics · 2026Review
- Structural organization of p62 filaments and the cellular ultrastructure of calcium-rich p62-enwrapped lipid droplet cargo.Nature communications · 2025Article
- Novel Biallelic SQSTM1 Mutation Causing a Subacute-Onset Complex Movement Disorder with Oculomotor Abnormalities.Movement disorders clinical practice · 2025Article
- A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy.Nature cell biology · 2025Article
- Cleavage of the selective autophagy receptor NBR1 by the PDCoV main protease NSP5 impairs autophagic degradation of the viral envelope protein.Autophagy · 2025Article
- KEAP1 retention in phase-separated p62 bodies drives liver damage under autophagy-deficient conditions.EMBO reports · 2025Article
- SUMOylation facilitates the stability of BCR-ABL to promote chronic myeloid leukemia progression.Oncogene · 2025Article
- Phase Separation: Orchestrating Biological Adaptations to Environmental Fluctuations.International journal of molecular sciences · 2025Review
- Interferon-induced PARP14-mediated ADP-ribosylation in p62 bodies requires the ubiquitin-proteasome system.The EMBO journal · 2025Article
- The LC3-interacting region of NBR1 is a protein interaction hub enabling optimal flux.The Journal of cell biology · 2025Article
- High-dimensional proteomic analysis for pathophysiological classification of traumatic brain injury.Brain : a journal of neurology · 2025Article
- Autophagy in erectile dysfunction: focusing on apoptosis and fibrosis.Asian journal of andrology · 2025Review
- Review
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p62/SQSTM1 is an autophagy receptor and signaling adaptor with an N-terminal PB1 domain that forms the scaffold of phase-separated p62 bodies in the cell. The molecular determinants that govern PB1 domain filament formation in vitro remain to be determined and the role of p62 filaments inside the cell is currently unclear. We here determine four high-resolution cryo-EM structures of different human and Arabidopsis PB1 domain assemblies and observed a filamentous ultrastructure of p62/SQSTM1 bodies using correlative cellular EM. We show that oligomerization or polymerization, driven by a double arginine finger in the PB1 domain, is a general requirement for lysosomal targeting of p62. Furthermore, the filamentous assembly state of p62 is required for autophagosomal processing of the p62-specific cargo KEAP1. Our results show that using such mechanisms, p62 filaments can be critical for cargo uptake in autophagy and are an integral part of phase-separated p62 bodies.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.