ArticleThe Journal of biological chemistry2013
Placing a disrupted degradation motif at the C terminus of proteasome substrates attenuates degradation without impairing ubiquitylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Conserved degronome features governing quality control associated proteolysis.Nature communications · 2022Article
- Mapping the degradation pathway of a disease-linked aspartoacylase variant.PLoS genetics · 2021Article
- Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope.Seminars in cell & developmental biology · 2019Review
- The Hunt for Degrons of the 26S Proteasome.Biomolecules · 2019Review
- Spatial Organization of Proteasome Aggregates in the Regulation of Proteasome Homeostasis.Frontiers in molecular biosciences · 2019Review
- Studying Spatial Protein Quality Control, Proteopathies, and Aging Using Different Model Misfolding Proteins inFrontiers in molecular neuroscience · 2018Review
- A Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.The Journal of biological chemistry · 2016Article
- Protein quality control in the nucleus.Current opinion in cell biology · 2016Review
- Distinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation.Biomolecules · 2014Review
- Reporter-based growth assay for systematic analysis of protein degradation.Journal of visualized experiments : JoVE · 2014Article
- Cellular maintenance of nuclear protein homeostasis.Cellular and molecular life sciences : CMLS · 2014Review
- Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Molecular biology of the cell · 2013Article
- Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein elimination by the ubiquitin-proteasome system requires the presence of a cis-acting degradation signal. Efforts to discern degradation signals of misfolded proteasome substrates thus far revealed a general mechanism whereby the exposure of cryptic hydrophobic motifs provides a degradation determinant. We have previously characterized such a determinant, employing the yeast kinetochore protein Ndc10 as a model substrate. Ndc10 is essentially a stable protein that is rapidly degraded upon exposure of a hydrophobic motif located at the C-terminal region. The degradation motif comprises two distinct and essential elements: DegA, encompassing two amphipathic helices, and DegB, a hydrophobic sequence within the loosely structured C-terminal tail of Ndc10. Here we show that the hydrophobic nature of DegB is irrelevant for the ubiquitylation of substrates containing the Ndc10 degradation motif, but is essential for proteasomal degradation. Mutant DegB, in which the hydrophobic sequence was disrupted, acted as a dominant degradation inhibitory element when expressed at the C-terminal regions of ubiquitin-dependent and -independent substrates of the 26S proteasome. This mutant stabilized substrates in both yeast and mammalian cells, indicative of a modular recognition moiety. The dominant function of the mutant DegB provides a powerful experimental tool for evaluating the physiological implications of stabilization of specific proteasome substrates in intact cells and for studying the associated pathological effects.
Indexed as
Identifiers
What OpenQuestion holds
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.