Evidence map›Paper›PMID 24489039›Full record

ArticleEukaryotic cell2014

Two-component histidine phosphotransfer protein Ypd1 is not essential for viability in Candida albicans.

John Mavrianos, Chirayu Desai, Neeraj Chauhan

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Oxidative Stress-Responsive Cell Wall Remodeling Depends on Phosphate inbioRxiv : the preprint server for biology · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Nutrient and Stress Sensing in Pathogenic Yeasts.Frontiers in microbiology · 2019
    Review
  16. Stress-Activated Protein Kinases in Human Fungal Pathogens.Frontiers in cellular and infection microbiology · 2019
    Review
  17. Acetylation of BcHpt Lysine 161 RegulatesFrontiers in microbiology · 2019
    Article
  18. Article
  19. Article
  20. The yeasts phosphorelay systems: a comparative view.World journal of microbiology & biotechnology · 2017
    Review
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

3 authors at 1 institution in 1 country.

John MavrianosPublic Health Research Institute, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, New Jersey, USA.
Chirayu Desai
Neeraj Chauhan
Rutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prokaryotes and lower eukaryotes, such as yeasts, utilize two-component signal transduction pathways to adapt cells to environmental stress and to regulate the expression of genes associated with virulence. One of the central proteins in this type of signaling mechanism is the phosphohistidine intermediate protein Ypd1. Ypd1 is reported to be essential for viability in the model yeast Saccharomyces cerevisiae. We present data here showing that this is not the case for Candida albicans. Disruption of YPD1 causes cells to flocculate and filament constitutively under conditions that favor growth in yeast form. To determine the function of Ypd1 in the Hog1 mitogen-activated protein kinase (MAPK) pathway, we measured phosphorylation of Hog1 MAPK in ypd1Δ/Δ and wild-type strains of C. albicans. Constitutive phosphorylation of Hog1 was observed in the ypd1Δ/Δ strain compared to the wild-type strain. Furthermore, fluorescence microscopy revealed that green fluorescent protein (GFP)-tagged Ypd1 is localized to both the nucleus and the cytoplasm. The subcellular segregation of GFP-tagged Ypd1 hints at an important role(s) of Ypd1 in regulation of Ssk1 (cytosolic) and Skn7 (nuclear) response regulator proteins via phosphorylation in C. albicans. Overall, our findings have profound implications for a mechanistic understanding of two-component signaling pathways in C. albicans, and perhaps in other pathogenic fungi.

Indexed as

Gene Expression Regulation, FungalSignal TransductionAmino Acid SequenceCandida albicansFungal ProteinsGene DeletionGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsIsoenzymesMicrobial ViabilityMitogen-Activated Protein KinasesMolecular Sequence DataPhosphorylationProtein KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiaeFungal ProteinsGreen Fluorescent ProteinsHOG1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsIsoenzymesMitogen-Activated Protein KinasesProtein KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSSK1 protein, Candida albicansYPD1 protein, S cerevisiae

Identifiers

PMID24489039
PMCPMC4000104
OpenAlexW1991100532

What Socratic 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 Socratic graph.