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Selective autophagic clearance of protein aggregates is mediated by the autophagy receptor, TAX1BP1

https://doi.org/10.1101/558767
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/j.ceb.2010.10.010openalex-snapshot
Protein misfolding disorders and macroautophagy
inferredcites →https://doi.org/10.1016/j.cell.2007.10.035openalex-snapshot
Homeostatic Levels of p62 Control Cytoplasmic Inclusion Body Formation in Autophagy-Deficient Mice
inferredcites →https://doi.org/10.1016/j.cell.2011.10.026openalex-snapshot
Autophagy: Renovation of Cells and Tissues
inferredcites →https://doi.org/10.1016/j.cell.2014.05.048openalex-snapshot
Autophagic Clearance of PolyQ Proteins Mediated by Ubiquitin-Atg8 Adaptors of the Conserved CUET Protein Family
inferredcites →https://doi.org/10.1016/j.cell.2016.07.001openalex-snapshot
UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome
inferredcites →https://doi.org/10.1016/j.devcel.2015.02.002openalex-snapshot
Neuronal Aggregates: Formation, Clearance, and Spreading
inferredcites →https://doi.org/10.1016/j.molcel.2004.12.021openalex-snapshot
Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation
inferredcites →https://doi.org/10.1016/j.molcel.2009.04.026openalex-snapshot
A Role for Ubiquitin in Selective Autophagy
inferredcites →https://doi.org/10.1016/j.molcel.2015.08.016openalex-snapshot
The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy
inferredcites →https://doi.org/10.1016/j.nbd.2010.08.015openalex-snapshot
The elimination of accumulated and aggregated proteins: A role for aggrephagy in neurodegeneration
inferredcites →https://doi.org/10.1016/j.stemcr.2017.08.019openalex-snapshot
Scalable Production of iPSC-Derived Human Neurons to Identify Tau-Lowering Compounds by High-Content Screening
inferredcites →https://doi.org/10.1016/s0896-6273(01)00177-5openalex-snapshot
Cellular Defenses against Unfolded Proteins
inferredcites →https://doi.org/10.1016/s0962-8924(00)01852-3openalex-snapshot
Aggresomes, inclusion bodies and protein aggregation
inferredcites →https://doi.org/10.1038/cr.2013.168openalex-snapshot
The machinery of macroautophagy
inferredcites →https://doi.org/10.1038/nature04723openalex-snapshot
Loss of autophagy in the central nervous system causes neurodegeneration in mice
inferredcites →https://doi.org/10.1038/nature04724openalex-snapshot
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
inferredcites →https://doi.org/10.1038/nature05291openalex-snapshot
The roles of intracellular protein-degradation pathways in neurodegeneration
inferredcites →https://doi.org/10.1038/nature14498openalex-snapshot
Regulation of endoplasmic reticulum turnover by selective autophagy
inferredcites →https://doi.org/10.1038/nature14893openalex-snapshot
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
inferredcites →https://doi.org/10.1038/ncb1723openalex-snapshot
Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
inferredcites →https://doi.org/10.1038/nchembio.1563openalex-snapshot
Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models
inferredcites →https://doi.org/10.1038/ni.2066openalex-snapshot
The kinase IKKα inhibits activation of the transcription factor NF-κB by phosphorylating the regulatory molecule TAX1BP1
inferredcites →https://doi.org/10.1038/sj.emboj.7601823openalex-snapshot
Essential role for TAX1BP1 in the termination of TNF‐α‐, IL‐1‐ and LPS‐mediated NF‐κB and JNK signaling
inferredcites →https://doi.org/10.1073/pnas.0505801102openalex-snapshot
Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
inferredcites →https://doi.org/10.1073/pnas.0802082105openalex-snapshot
A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
inferredcites →https://doi.org/10.1073/pnas.0912417107openalex-snapshot
TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
inferredcites →https://doi.org/10.1073/pnas.1405752111openalex-snapshot
Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
inferredcites →https://doi.org/10.1073/pnas.97.4.1589openalex-snapshot
Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
inferredcites →https://doi.org/10.1074/jbc.m609532200openalex-snapshot
Trehalose, a Novel mTOR-independent Autophagy Enhancer, Accelerates the Clearance of Mutant Huntingtin and α-Synuclein
inferredcites →https://doi.org/10.1080/07391102.2014.951688openalex-snapshot
Crystallographic and modelling studies suggest that the SKICH domains from different protein families share a common Ig-like fold but harbour substantial structural variations
inferredcites →https://doi.org/10.1083/jcb.200507002openalex-snapshot
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
inferredcites →https://doi.org/10.1084/jem.20150956openalex-snapshot
Therapeutic targeting of autophagy in neurodegenerative and infectious diseases
inferredcites →https://doi.org/10.1091/mbc.8.8.1559openalex-snapshot
Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells.
inferredcites →https://doi.org/10.1093/bioinformatics/btq046openalex-snapshot
EBImage—an R package for image processing with applications to cellular phenotypes
inferredcites →https://doi.org/10.1093/hmg/11.9.1107openalex-snapshot
Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
inferredcites →https://doi.org/10.1093/hmg/ddq093openalex-snapshot
Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington's disease
inferredcites →https://doi.org/10.1101/cshperspect.a006734openalex-snapshot
Integration of Clearance Mechanisms: The Proteasome and Autophagy
inferredcites →https://doi.org/10.1101/gad.1657108openalex-snapshot
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
inferredcites →https://doi.org/10.1107/s2053230x14006396openalex-snapshot
Expression, purification and crystallization of the SKICH domain of human TAX1BP1
inferredcites →https://doi.org/10.1111/j.1460-9568.2011.07803.xopenalex-snapshot
Genetic strategies to study TDP-43 in rodents and to develop preclinical therapeutics for amyotrophic lateral sclerosis
inferredcites →https://doi.org/10.1111/j.1742-4658.2008.06562.xopenalex-snapshot
Huntington’s disease: degradation of mutant huntingtin by autophagy
inferredcites →https://doi.org/10.1128/mcb.01485-08openalex-snapshot
Selective Accumulation of Aggregation-Prone Proteasome Substrates in Response to Proteotoxic Stress
inferredcites →https://doi.org/10.1146/annurev.biochem.67.1.425openalex-snapshot
THE UBIQUITIN SYSTEM
inferredcites →https://doi.org/10.1155/2011/732798openalex-snapshot
Autophagy in Inflammatory Diseases
inferredcites →https://doi.org/10.1155/2012/282041openalex-snapshot
Lipophagy: Connecting Autophagy and Lipid Metabolism
inferredcites →https://doi.org/10.1155/2012/673290openalex-snapshot
Receptor Proteins in Selective Autophagy
inferredcites →https://doi.org/10.1155/2012/736905openalex-snapshot
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
inferredcites →https://doi.org/10.1172/jci58656openalex-snapshot
The immunology of neurodegeneration
inferredcites →https://doi.org/10.1186/gb-2006-7-10-r100openalex-snapshot
CellProfiler: image analysis software for identifying and quantifying cell phenotypes
inferredcites →https://doi.org/10.1371/journal.pone.0146021openalex-snapshot
Dose-Response Analysis Using R
inferredcites →https://doi.org/10.1371/journal.ppat.1005174openalex-snapshot
The Autophagy Receptor TAX1BP1 and the Molecular Motor Myosin VI Are Required for Clearance of Salmonella Typhimurium by Autophagy
inferredcites →https://doi.org/10.1371/journal.ppat.1005433openalex-snapshot
Correction: The Autophagy Receptor TAX1BP1 and the Molecular Motor Myosin VI Are Required for Clearance of Salmonella Typhimurium by Autophagy
inferredcites →https://doi.org/10.1523/jneurosci.2911-10.2010openalex-snapshot
Phosphorylation Promotes Neurotoxicity in aCaenorhabditis elegansModel of TDP-43 Proteinopathy
inferredcites →https://doi.org/10.1523/jneurosci.4988-09.2010openalex-snapshot
Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis
inferredcites →https://doi.org/10.2298/csis0501103hopenalex-snapshot
FP-outlier: Frequent pattern based outlier detection
inferredcites →https://doi.org/10.3389/fnins.2017.00185openalex-snapshot
Protein Quality Control by Molecular Chaperones in Neurodegeneration
inferredcites →https://doi.org/10.4049/jimmunol.157.5.1823openalex-snapshot
Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules?
inferredcites →https://doi.org/10.4161/auto.5.5.8566openalex-snapshot
NBR1 co-operates with p62 in selective autophagy of ubiquitinated targets
inferredcites →https://doi.org/10.4161/auto.6.2.11118openalex-snapshot
NDP52, a novel autophagy receptor for ubiquitin-decorated cytosolic bacteria
inferredcites →https://doi.org/10.4161/auto.7.3.14046openalex-snapshot
The ubiquitin-binding adaptor proteins p62/SQSTM1 and NDP52 are recruited independently to bacteria-associated microdomains to target Salmonella to the autophagy pathway
inferredcites →https://doi.org/10.4161/cc.8.13.8892openalex-snapshot
NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.ajpath.2023.02.015openalex-snapshot
SQSTM1/p62 and Hepatic Mallory-Denk Body Formation in Alcohol-Associated Liver Disease
inferred← citeshttps://doi.org/10.1016/j.mam.2021.100973openalex-snapshot
Autophagy in liver diseases: A review
inferred← citeshttps://doi.org/10.1016/j.mito.2021.01.001openalex-snapshot
Mitophagy impairment in neurodegenerative diseases: Pathogenesis and therapeutic interventions
inferred← citeshttps://doi.org/10.1038/s41418-020-00667-xopenalex-snapshot
Ubiquitin signaling in neurodegenerative diseases: an autophagy and proteasome perspective
inferred← citeshttps://doi.org/10.1080/15548627.2022.2039535openalex-snapshot
Chloroquine treatment induces secretion of autophagy-related proteins and inclusion of Atg8-family proteins in distinct extracellular vesicle populations
inferred← citeshttps://doi.org/10.1080/19490976.2025.2534677openalex-snapshot
Harnessing Lactiplantibacillus plantarum EP21 and its membrane vesicles to inhibit myopia development
inferred← citeshttps://doi.org/10.1101/2020.07.07.191189openalex-snapshot
FIP200 organizes the autophagy machinery at p62-ubiquitin condensates beyond activation of the ULK1 kinase
inferred← citeshttps://doi.org/10.1111/febs.15617openalex-snapshot
Alternative systems for misfolded protein clearance: life beyond the proteasome
inferred← citeshttps://doi.org/10.15252/embj.2020104948openalex-snapshot
Receptor‐mediated clustering of FIP200 bypasses the role of LC3 lipidation in autophagy
inferred← citeshttps://doi.org/10.3389/fcell.2021.660626openalex-snapshot
Proteostasis in the Male and Female Germline: A New Outlook on the Maintenance of Reproductive Health
inferred← citeshttps://doi.org/10.70675/ce9204b1z17c7z476bz9bd5z4e801e0613efopenalex-snapshot
The nuclear protein quality control system for the elimination of stress-induced aggregates
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