Evidence map›Paper›PMID 16096648›Full record

ArticleThe EMBO journal2005

AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism.

Penghua Wang, Yong Zhang, Hongzhe Li, Hai Kee Chieu, Alan L Munn, Hongyuan Yang

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. A detour for yeast oxysterol binding proteins.The Journal of biological chemistry · 2012
    Review
  11. Article
  12. Article
  13. Article
  14. The diverse functions of oxysterol-binding proteins.Annual review of cell and developmental biology · 2010
    Review
  15. Article
  16. The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. Review
  18. Biogenesis and function of multivesicular bodies.Annual review of cell and developmental biology · 2007
    Review
  19. 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

6 authors at 2 institutions in 2 countries.

Penghua WangDepartment of Biochemistry, Faculty of Medicine, National University of Singapore, Singapore, Singapore.
Yong Zhang
Hongzhe Li
Hai Kee Chieu
Alan L Munn
Hongyuan Yang
National University of Singapore · SGUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast genome encodes seven oxysterol binding protein homologs, Osh1p-Osh7p, which have been implicated in regulating intracellular lipid and vesicular transport. Here, we show that both Osh6p and Osh7p interact with Vps4p, a member of the AAA (ATPases associated with a variety of cellular activities) family. The coiled-coil domain of Osh7p was found to interact with Vps4p in a yeast two-hybrid screen and the interaction between Osh7p and Vps4p appears to be regulated by ergosterol. Deletion of VPS4 induced a dramatic increase in the membrane-associated pools of Osh6p and Osh7p and also caused a decrease in sterol esterification, which was suppressed by overexpression of OSH7. Lastly, overexpression of the coiled-coil domain of Osh7p (Osh7pCC) resulted in a multivesicular body sorting defect, suggesting a dominant negative role of Osh7pCC possibly through inhibiting Vps4p function. Our data suggest that a common mechanism may exist for AAA proteins to regulate the membrane association of yeast OSBP proteins and that these two protein families may function together to control subcellular lipid transport.

Indexed as

Adenosine TriphosphatasesCarrier ProteinsCell MembraneEndosomal Sorting Complexes Required for TransportEstersFatty Acid-Binding ProteinsMutationOxysterol Binding ProteinsProtein BindingProtein Structure, TertiaryReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSterolsTwo-Hybrid System TechniquesAdenosine TriphosphatasesCarrier ProteinsEndosomal Sorting Complexes Required for TransportEstersFatty Acid-Binding ProteinsOsh7 protein, S cerevisiaeOxysterol Binding ProteinsReceptors, SteroidSaccharomyces cerevisiae ProteinsSterolsVPS4 protein, S cerevisiae

Identifiers

PMID16096648
PMCPMC1201346
OpenAlexW2100349219

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.