ArticleThe Journal of biological chemistry2015
Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 25 citations in OpenAlex.
- Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.Cellular and molecular life sciences : CMLS · 2023Article
- Deciphering non-canonical ubiquitin signaling: biology and methodology.Frontiers in molecular biosciences · 2023Review
- Thioester and Oxyester Linkages in the Ubiquitin System.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Endoplasmic Reticulum-Associated Protein Degradation.Cold Spring Harbor perspectives in biology · 2022Review
- Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022Review
- Strategies to Better Target Fungal Squalene Monooxygenase.Journal of fungi (Basel, Switzerland) · 2021Review
- Nuclear Ubiquitin-Proteasome Pathways in Proteostasis Maintenance.Biomolecules · 2021Review
- Disposing of misfolded ER proteins: A troubled substrate's way out of the ER.Molecular and cellular endocrinology · 2020Review
- Regulation of inner nuclear membrane associated protein degradation.Nucleus (Austin, Tex.) · 2019Review
- Cellular functions and molecular mechanisms of non-lysine ubiquitination.Open biology · 2019Review
- Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins.Scientific reports · 2019Article
- Mechanisms and functions of ribosome-associated protein quality control.Nature reviews. Molecular cell biology · 2019Review
- Non-canonical ubiquitination of the cholesterol-regulated degron of squalene monooxygenase.The Journal of biological chemistry · 2019Article
- The host cell ubiquitin ligase protein CHIP is a potent suppressor of HIV-1 replication.The Journal of biological chemistry · 2019Article
- Isopeptide and ester bond ubiquitination both regulate degradation of the human dopamine receptor 4.The Journal of biological chemistry · 2017Article
- E2 enzymes: more than just middle men.Cell research · 2016Review
- Degradation-mediated protein quality control at the inner nuclear membrane.Nucleus (Austin, Tex.) · 2016Review
- Lysine Residues Are Not Required for Proteasome-Mediated Proteolysis of the Auxin/Indole Acidic Acid Protein IAA1.Plant physiology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proteins are typically targeted for proteasomal degradation by the attachment of a polyubiquitin chain to ϵ-amino groups of lysine residues. Non-lysine ubiquitylation of proteasomal substrates has been considered an atypical and rare event limited to complex eukaryotes. Here we report that a fully functional lysine-less mutant of an inner nuclear membrane protein in yeast, Asi2, is polyubiquitylated and targeted for proteasomal degradation. Efficient degradation of lysine-free Asi2 requires E3-ligase Doa10 and E2 enzymes Ubc6 and Ubc7, components of the endoplasmic reticulum-associated degradation pathway. Together, our data suggest that non-lysine ubiquitylation may be more prevalent than currently considered.
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.