Evidence map›Paper›PMID 19805280›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation.

Gang Zhao, Guangtao Li, Hermann Schindelin, William J Lennarz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Doa1 is a MAD adaptor for Cdc48.The Journal of cell biology · 2016
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Cdc48: a swiss army knife of cell biology.Journal of amino acids · 2013
    Review
  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

4 authors at 2 institutions in 2 countries.

Gang ZhaoCenter for Structural Biology and Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Guangtao Li
Hermann Schindelin
William J Lennarz
Stony Brook University · USUniversity of Würzburg · DE

Funding

The Molybdenum Cofactor: Biosynthesis and FunctionR01DK054835 · NIDDK · STATE UNIVERSITY NEW YORK STONY BROOK · PI SCHINDELIN, HERMANN · 1999 to 2007
$2.1M
NIDDK NIH HHS DK54835NIDDK NIH HHS R01 DK054835NIGMS NIH HHS GM33814
6 · The paper itself

Abstract

The yeast AAA-ATPase Cdc48 and the ubiquitin fusion degradation (UFD) proteins play important, evolutionarily conserved roles in ubiquitin dependent protein degradation. The N-terminal domain of Cdc48 interacts with substrate-recruiting cofactors, whereas the C terminus of Cdc48 binds to proteins such as Ufd3 that process substrates. Ufd3 is essential for efficient protein degradation and for maintaining cellular ubiquitin levels. This protein contains an N-terminal WD40 domain, a central ubiquitin-binding domain, and a C-terminal Cdc48-binding PUL domain. The crystal structure of the PUL domain reveals an Armadillo repeat with high structural similarity to importin-alpha, and the Cdc48-binding site could be mapped to the concave surface of the PUL domain by biochemical studies. Alterations of the Cdc48 binding site of Ufd3 by site-directed mutagenesis resulted in a depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. Therefore, our data provide direct evidence that the functions of Ufd3 in ubiquitin homeostasis and protein degradation depend on its interaction with the C terminus of Cdc48.

Indexed as

Amino Acid MotifsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesAmino Acid SequenceAnimalsArmadillo Domain ProteinsBinding SitesCell Cycle ProteinsFluorometryHomeostasisHydrolysisImmunoblottingImmunoprecipitationModels, MolecularMolecular Sequence DataMutationAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesArmadillo Domain ProteinsCDC48 protein, S cerevisiaeCell Cycle ProteinsDOA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinValosin Containing Protein

Identifiers

PMID19805280
PMCPMC2752524
OpenAlexW2114291232

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.