Evidence map›Paper›PMID 19915539›Full record

ArticleNature chemical biology2009

Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis.

Amparo Ruiz, Asier González, Ivan Muñoz, Raquel Serrano, J Albert Abrie, Erick Strauss, Joaquín Ariño

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In one paragraph

Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Moonlighting Proteins: Diverse Functions Found in Fungi.Journal of fungi (Basel, Switzerland) · 2023
    Review
  4. Article
  5. Article
  6. Fungal Hal3 (and Its Close Relative Cab3) as Moonlighting Proteins.Journal of fungi (Basel, Switzerland) · 2022
    Review
  7. When Phosphatases Go Mad: The Molecular Basis for Toxicity of Yeast Ppz1.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells.International journal of molecular sciences · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. The Expanding Landscape of Moonlighting Proteins in Yeasts.Microbiology and molecular biology reviews : MMBR · 2016
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

Amparo RuizDepartament de Bioquimica i Biologia Molecular, Universitat Autònoma de Barcelona, Spain.
Asier González
Ivan Muñoz
Raquel Serrano
J Albert Abrie
Erick Strauss
Joaquín Ariño
Universitat Autònoma de Barcelona · ESStellenbosch University · ZAColumbia University · USMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Unlike most other organisms, the essential five-step coenzyme A biosynthetic pathway has not been fully resolved in yeast. Specifically, the genes encoding the phosphopantothenoylcysteine decarboxylase (PPCDC) activity still remain unidentified. Sequence homology analyses suggest three candidates-Ykl088w, Hal3 and Vhs3-as putative PPCDC enzymes in Saccharomyces cerevisiae. Notably, Hal3 and Vhs3 have been characterized as negative regulatory subunits of the Ppz1 protein phosphatase. Here we show that YKL088w does not encode a third Ppz1 regulatory subunit, and that the essential roles of Ykl088w and the Hal3 and Vhs3 pair are complementary, cannot be interchanged and can be attributed to PPCDC-related functions. We demonstrate that while known eukaryotic PPCDCs are homotrimers, the active yeast enzyme is a heterotrimer that consists of Ykl088w and Hal3/Vhs3 monomers that separately provides two essential catalytic residues. Our results unveil Hal3 and Vhs3 as moonlighting proteins involved in both CoA biosynthesis and protein phosphatase regulation.

Indexed as

Base SequenceCarboxy-LyasesCell Cycle ProteinsCoenzyme ACrystallography, X-RayModels, MolecularMolecular Sequence DataPhosphoprotein PhosphatasesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarboxy-LyasesCell Cycle ProteinsCoenzyme APhosphopantothenoyl-cysteine decarboxylasePhosphoprotein PhosphatasesPPZ1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIS2 protein, S cerevisiaeVHS3 protein, S cerevisiae

Identifiers

PMID19915539
OpenAlexW2114437179

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.