Evidence map›Paper›PMID 20159987›Full record

ArticleThe Journal of biological chemistry2010

Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates.

Chang Liu, Dewald van Dyk, Ping Xu, Vitnary Choe, Haihui Pan, Junmin Peng, Brenda Andrews, Hai Rao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
    Review
  4. Review
  5. Article
  6. Ubiquitination in the ERAD Process.International journal of molecular sciences · 2020
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Cdc48: a swiss army knife of cell biology.Journal of amino acids · 2013
    Review
  14. Article
  15. Review
  16. Article
  17. Type 2 deiodinase at the crossroads of thyroid hormone action.The international journal of biochemistry & cell biology · 2011
    Review
  18. The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Article
  20. 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

8 authors at 3 institutions in 2 countries.

Chang LiuInstitute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245, USA.
Dewald van Dyk
Ping Xu
Vitnary Choe
Haihui Pan
Junmin Peng
Brenda Andrews
Hai Rao
The University of Texas Health Science Center at San Antonio · USEmory University · USUniversity of Toronto · CA

Funding

Targeting ubiquitylated proteins to the proteasomeR01GM078085 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI RAO, HAI · 2007 to 2011
$1.3M
NIGMS NIH HHS GM 078085NIGMS NIH HHS R01 GM078085
6 · The paper itself

Abstract

Ufd2 is the founding member of E4 enzymes that are specifically involved in ubiquitin chain elongation but whose roles in proteolysis remain scarce. Here, using a genome-wide screen, we identified one cellular target of yeast Ufd2 as the membrane protein Pex29. The ubiquitin chains assembled on Pex29 in vivo by Ufd2 mainly contain Lys-48 linkages. We found that the ubiquitin-protein E3 ligase for overexpressed Pex29 is Doa10, which is known to be involved in protein quality control. Interestingly, not all Doa10 substrates are regulated by Ufd2, suggesting that E4 involvement is not specific to a particular E3, but may depend on the spatial arrangement of the E3-substrate interaction. Cells lacking UFD2 elicit an unfolded protein response, expanding the physiological function of Ufd2. Our results lead to novel insights into the biological role of Ufd2 and further underscore the significance of Ufd2 in proteolysis.

Indexed as

ImmunoblottingLysineMembrane ProteinsPlasmidsProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUnfolded Protein ResponseLysineMembrane ProteinsPEX29 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSSM4 protein, S cerevisiaeUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUFD2 protein, S cerevisiae

Identifiers

PMID20159987
PMCPMC2856231
OpenAlexW1994077412

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.