ArticleThe Journal of cell biology2016
Protein misfolding specifies recruitment to cytoplasmic inclusion bodies.
Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 40 citations in OpenAlex.
- SMURF2 attenuates NRF2-driven tumor progression by acting as a nuclear brake on NRF2 during cellular stress.Redox biology · 2026Article
- Episodic transport of protein aggregates achieves a positive size selectivity in aggresome formation.Nature communications · 2025Article
- Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response.Diseases (Basel, Switzerland) · 2023Review
- LISTERIN E3 Ubiquitin Ligase and Ribosome-Associated Quality Control (RQC) Mechanism.Molecular neurobiology · 2021Review
- The p97-UBXN1 complex regulates aggresome formation.Journal of cell science · 2021Article
- Stress-induced NEDDylation promotes cytosolic protein aggregation through HDAC6 in a p62-dependent manner.iScience · 2021Article
- Formation of Biomolecular Condensates in Bacteria by Tuning Protein Electrostatics.ACS central science · 2020Article
- K63-linked ubiquitylation induces global sequestration of mitochondria.Scientific reports · 2020Article
- AggreCount: an unbiased image analysis tool for identifying and quantifying cellular aggregates in a spatially defined manner.The Journal of biological chemistry · 2020Article
- Parkinson's disease and translational research.Translational neurodegeneration · 2020Review
- The Cdc48 Complex Alleviates the Cytotoxicity of Misfolded Proteins by Regulating Ubiquitin Homeostasis.Cell reports · 2020Article
- Selective autophagy of cytosolic protein aggregates involves ribosome-free rough endoplasmic reticulum.Histochemistry and cell biology · 2020Article
- Strategies to Investigate Ubiquitination in Huntington's Disease.Frontiers in chemistry · 2020Review
- Acute unfolding of a single protein immediately stimulates recruitment of ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes.The Journal of biological chemistry · 2019Article
- Quality Control in Huntington's Disease: a Therapeutic Target.Neurotoxicity research · 2019Review
- Nascent-protein ubiquitination is required for heat shock-induced gene downregulation in human cells.Nature structural & molecular biology · 2019Article
- Targeting the proteostasis network in Huntington's disease.Ageing research reviews · 2019Review
- N-terminal fusion potentiates α-synuclein secretion [correction].Cellular and molecular neurobiology · 2018Review
- TRIM16 controls assembly and degradation of protein aggregates by modulating the p62-NRF2 axis and autophagy.The EMBO journal · 2018Article
- Nuclear export of ubiquitinated proteins via the UBIN-POST system.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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3 authors at 2 institutions in 2 countries.
Funding
Abstract
Inclusion bodies (IBs) containing aggregated disease-associated proteins and polyubiquitin (poly-Ub) conjugates are universal histopathological features of neurodegenerative diseases. Ub has been proposed to target proteins to IBs for degradation via autophagy, but the mechanisms that govern recruitment of ubiquitylated proteins to IBs are not well understood. In this paper, we use conditionally destabilized reporters that undergo misfolding and ubiquitylation upon removal of a stabilizing ligand to examine the role of Ub conjugation in targeting proteins to IBs that are composed of an N-terminal fragment of mutant huntingtin, the causative protein of Huntington's disease. We show that reporters are excluded from IBs in the presence of the stabilizing ligand but are recruited to IBs after ligand washout. However, we find that Ub conjugation is not necessary to target reporters to IBs. We also report that forced Ub conjugation by the Ub fusion degradation pathway is not sufficient for recruitment to IBs. Finally, we find that reporters and Ub conjugates are stable at IBs. These data indicate that compromised folding states, rather than conjugation to Ub, can specify recruitment to IBs.
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Registered trials
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.