Aggresomes, inclusion bodies and protein aggregation.
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Summary
This work has suggested that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules and this microtubule-dependent inclusion body is called an aggresome.
- Type
- review
- Published
- 2000-12-01
- Cited by
- 1,992
- References
- 46
- OpenAlex
- https://openalex.org/W1988146888
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24294639
Keywords
Aggresome, Biology, Inclusion bodies, Protein aggregation, Cell biology
References
- The latent membrane protein‐1 in Epstein‐Barr virus‐transformed lymphoblastoid cells is found with ubiquitin‐protein conjugates and heat‐shock protein 70 in lysosomes oriented around the microtubule organizing centre
- Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome.
- Subpopulations of proteasomes in rat liver nuclei, microsomes and cytosol.
- An inhibitor of the chymotrypsin-like activity of the proteasome (PSI) induces similar morphological changes in various cell lines.
- On the spatial organization of ubiquitin-dependent proteolysis in HeLa cells.
- Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation.
- Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers.
- Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins.
- Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
- Intermediate filament-ubiquitin diseases: implications for cell sanitization.
- Protein aggregation: folding aggregates, inclusion bodies and amyloid.
- ER quality control: the cytoplasmic connection.
- Mutations and off-pathway aggregation of proteins.
- Human thyroperoxidase is largely retained and rapidly degraded in the endoplasmic reticulum. Its N-glycans are required for folding and intracellular trafficking.
- The role of motor proteins in establishing the microtubule arrays of axons and dendrites.
- Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
- Export from the Endoplasmic Reticulum Represents the Limiting Step in the Maturation and Cell Surface Expression of the Human δ Opioid Receptor*
- Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation.
- PMP22 accumulation in aggresomes: implications for CMT1A pathology.
- Recognition of the polyubiquitin proteolytic signal
Cited by
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- Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex.
- Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled.
- A mechanism of macroscopic (amorphous) aggregation of the tobacco mosaic virus coat protein.
- Molecular genetics approaches in yeast to study amyloid diseases
- Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB.
- Cutting Edge: Microbial Products Elicit Formation of Dendritic Cell Aggresome-Like Induced Structures in Macrophages1
- A new frontier in pharmacology: the endoplasmic reticulum as a regulated export pathway in health and disease
- Inhibition of protein crystallization by evolutionary negative design
- Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a prefibrillar, highly cytotoxic state
- Capturing protein-protein complexes at equilibrium: the holdup comparative chromatographic retention assay.
- Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay.
- Oxidative stress induces the endoplasmic reticulum stress and facilitates inclusion formation in cultured cells.
- Effect of Proteasome Inhibitors With Different Chemical Structures on the Ubiquitin–Proteasome System In Vitro
- BAG3 mediates chaperone‐based aggresome‐targeting and selective autophagy of misfolded proteins
- Kinetics of Inclusion Body Formation and Its Correlation with the Characteristics of Protein Aggregates in Escherichia coli
- Polycystin-1 Cleavage and the Regulation of Transcriptional Pathways
- Self-assembling amphipathic alpha-helical peptides induce the formation of active protein aggregates in vivo.
- When less becomes more: optimization of protein expression in HEK293-EBNA1 cells using plasmid titration - a case study for NLRs.
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