Evidence map›Paper›PMID 11805328›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome.

Minoru Funakoshi, Toru Sasaki, Takeharu Nishimoto, Hideki Kobayashi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

119 citing papers in PubMed, 243 citations in OpenAlex.

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  18. Protein Quality Control at the Mitochondrial Surface.Frontiers in cell and developmental biology · 2021
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59 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Minoru FunakoshiDepartment of Molecular Biology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
Toru Sasaki
Takeharu Nishimoto
Hideki Kobayashi
Kyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dsk2p from Saccharomyces cerevisiae belongs to the class of proteins that contain a ubiquitin-like (UbL) domain at the N terminus together with a ubiquitin-associated (UBA) domain at the C terminus. We show here that the C-terminal UBA domain of Dsk2p binds to K48-linked polyubiquitin chains, and the N-terminal UbL domain of Dsk2p interacts with the proteasome. Overexpression of Dsk2p caused the accumulation of large amounts of polyubiquitin, and extragenic suppressors of the Dsk2p-mediated lethality proved to be temperature-sensitive mutations in two proteasome subunits, rpn1 and pre2. K48-linked ubiquitin-dependent degradation was impaired by disruption of the DSK2 gene. These results indicate that Dsk2p is K48-linked polyubiquitin-binding protein and also interacts with the proteasome. We discuss a possible role of adaptor function of Dsk2p via its UbL and UBA domains in the ubiquitin-proteasome pathway.

Indexed as

Cell Cycle ProteinsBinding SitesCysteine EndopeptidasesDNA-Binding ProteinsFungal ProteinsGenes, FungalGenes, SuppressorMultienzyme ComplexesMutationProteasome Endopeptidase ComplexProteinsProtein Structure, TertiaryProtein SubunitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsTemperatureCell Cycle ProteinsCysteine EndopeptidasesDNA-Binding ProteinsDSK2 protein, S cerevisiaeFungal ProteinsMultienzyme ComplexesPRE2 protein, S cerevisiaeProteasome Endopeptidase ComplexProteinsProtein SubunitsRAD23 protein, S cerevisiaeRecombinant ProteinsRPN1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitins

Identifiers

PMID11805328
PMCPMC117376
OpenAlexW2062636623

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.