Evidence map›Paper›PMID 21976488›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.

Kojiro Takeda, Nam K Tonthat, Tiffany Glover, Weijun Xu, Eugene V Koonin, Mitsuhiro Yanagida, Maria A Schumacher

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Emerging Connections between Nuclear Pore Complex Homeostasis and ALS.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019
    Review
  9. Proteasomes tether to two distinct sites at the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Kojiro TakedaG0 Cell Unit, Okinawa Institute of Science and Technology, 1919-1 Tancha, Onna, Okinawa, Japan.
Nam K Tonthat
Tiffany Glover
Weijun Xu
Eugene V Koonin
Mitsuhiro Yanagida
Maria A Schumacher
Duke University Hospital · USOkinawa Institute of Science and Technology Graduate University · JPThe University of Texas MD Anderson Cancer Center · USNational Institutes of Health · US

Funding

Finding Protein Sequence Motifs--Methods And ApplicationsZIALM000061 · NLM · NATIONAL LIBRARY OF MEDICINE · PI KOONIN, EUGENE V · 2009 to 2025
$10.6M
Structural studies on the P1 plasmid partition apparatus.R01GM074815 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI SCHUMACHER, MARIA · 2006 to 2009
$720k
NIGMS NIH HHS GM074815NIGMS NIH HHS R01 GM074815
6 · The paper itself

Abstract

Degradation of nuclear proteins by the 26S proteasome is essential for cell viability. In yeast, the nuclear envelope protein Cut8 mediates nuclear proteasomal sequestration by an uncharacterized mechanism. Here we describe structures of Schizosaccharomyces pombe Cut8, which shows that it contains a unique, modular fold composed of an extended N-terminal, lysine-rich segment that when ubiquitinated binds the proteasome, a dimer domain followed by a six-helix bundle connected to a flexible C tail. The Cut8 six-helix bundle shows structural similarity to 14-3-3 phosphoprotein-binding domains, and binding assays show that this domain is necessary and sufficient for liposome and cholesterol binding. Moreover, specific mutations in the 14-3-3 regions corresponding to putative cholesterol recognition/interaction amino acid consensus motifs abrogate cholesterol binding. In vivo studies confirmed that the 14-3-3 region is necessary for Cut8 membrane localization and that dimerization is critical for its function. Thus, the data reveal the Cut8 organization at the nuclear envelope. Reconstruction of Cut8 evolution suggests that it was present in the last common ancestor of extant eukaryotes and accordingly that nuclear proteasomal sequestration is an ancestral eukaryotic feature. The importance of Cut8 for cell viability and its absence in humans suggests it as a possible target for the development of specific chemotherapeutics against invasive fungal infections.

Indexed as

14-3-3 ProteinsAmino Acid SequenceAmino Acid SubstitutionCell Cycle ProteinsCell NucleusConserved SequenceDimerizationEvolution, MolecularGenes, FungalModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhenotypeProteasome Endopeptidase ComplexProtein FoldingProtein Structure, Quaternary14-3-3 ProteinsCell Cycle ProteinsCut8 protein, S pombeProteasome Endopeptidase ComplexRecombinant ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID21976488
PMCPMC3193221
OpenAlexW1974499129

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.