ArticleProceedings of the National Academy of Sciences of the United States of America2013
Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 58 citations in OpenAlex.
- Article
- The YΦ motif defines the structure-activity relationships of human 20S proteasome activators.Nature communications · 2022Article
- Protein-protein interactions in plant antioxidant defense.Frontiers in plant science · 2022Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms.Biomolecules · 2020Review
- Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding.Science (New York, N.Y.) · 2019Article
- Proteasomes and Several Aspects of Their Heterogeneity Relevant to Cancer.Frontiers in oncology · 2019Review
- The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome.Communications biology · 2019Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Mechanistic insights into ER-associated protein degradation.Current opinion in cell biology · 2018Review
- Article
- Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase.Frontiers in molecular biosciences · 2018Review
- Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates.Molecular biology of the cell · 2017Article
- Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48.Scientific reports · 2017Article
- Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP•NPLOC4•UFD1L is enhanced by a mutation that causes multisystem proteinopathy.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Frontiers in molecular biosciences · 2017Review
- Toward an understanding of the Cdc48/p97 ATPase.F1000Research · 2017Review
- Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Proteasomes are essential and ubiquitous ATP-dependent proteases that function in eukarya, archaea, and some bacteria. These destructive but critically important proteolytic machines use a 20S core peptidase and a hexameric ATPase associated with a variety of cellular activities (AAA+) unfolding ring that unfolds and spools substrates into the peptidase chamber. In archaea, 20S can function with the AAA+ Cdc48 or proteasome-activating nucleotidase (PAN) unfoldases. Both interactions are stabilized by C-terminal tripeptides in AAA+ subunits that dock into pockets on the 20S periphery. Here, we provide evidence that archaeal Cdc48 also uses a distinct set of near-axial interactions to bind 20S and propose that similar dual determinants mediate PAN-20S interactions and Rpt(1-6)-20S interactions in the 26S proteasome. Current dogma holds that the Rpt(1-6) unfolding ring of the 19S regulatory particle is the only AAA+ partner of eukaryotic 20S. By contrast, we show that mammalian Cdc48, a key player in cell-cycle regulation, membrane fusion, and endoplasmic-reticulum-associated degradation, activates mammalian 20S and find that a mouse Cdc48 variant supports protein degradation in combination with 20S. Our results suggest that eukaryotic Cdc48 orthologs function directly with 20S to maintain intracellular protein quality control.
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.