Evidence map›Paper›PMID 21282602›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Polarity proteins Bem1 and Cdc24 are components of the filamentous fungal NADPH oxidase complex.

Daigo Takemoto, Sachiko Kamakura, Sanjay Saikia, Yvonne Becker, Ruth Wrenn, Aiko Tanaka, Hideki Sumimoto, Barry Scott

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  4. The Compatibility of theJournal of fungi (Basel, Switzerland) · 2026
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  6. Draft genome sequences ofMicrobiology resource announcements · 2024
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  7. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. NADPH Oxidases Play a Role in PathogenicityFrontiers in cellular and infection microbiology · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. The NADPH oxidase in Volvariella volvacea and its differential expression in response to mycelial ageing and mechanical injury.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Review
  19. Review
  20. Article

1 more citing papers are in PubMed but not listed here.

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 2 institutions in 3 countries.

Daigo TakemotoGraduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Sachiko Kamakura
Sanjay Saikia
Yvonne Becker
Ruth Wrenn
Aiko Tanaka
Hideki Sumimoto
Barry Scott
Massey University · NZKyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulated synthesis of reactive oxygen species (ROS) by membrane-bound fungal NADPH oxidases (Nox) plays a key role in fungal morphogenesis, growth, and development. Generation of reactive oxygen species (ROS) by the plant symbiotic fungus, Epichloë festucae, requires functional assembly of a multisubunit complex composed of NoxA, a regulatory component, NoxR, and the small GTPase RacA. However, the mechanism for assembly and activation of this complex at the plasma membrane is unknown. We found by yeast two-hybrid and coimmunoprecipitation assays that E. festucae NoxR interacts with homologs of the yeast polarity proteins, Bem1 and Cdc24, and that the Phox and Bem1 (PB1) protein domains found in these proteins are essential for these interactions. GFP fusions of BemA, Cdc24, and NoxR preferentially localized to actively growing hyphal tips and to septa. These proteins interact with each other in vivo at these same cellular sites as shown by bimolecular fluorescent complementation assays. The PB1 domain of NoxR is essential for localization to the hyphal tip. An E. festucae ΔbemA mutant was defective in hyphal morphogenesis and growth in culture and in planta. The changes in fungal growth in planta resulted in a defective symbiotic interaction phenotype. Our inability to isolate a Δcdc24 mutant suggests this gene is essential. These results demonstrate that BemA and Cdc24 play a critical role in localizing NoxR protein to sites of fungal hyphal morphogenesis and growth. Our findings identify a potential shared ancestral link between the protein machinery required for fungal polarity establishment and the Nox complex controlling cellular differentiation.

Indexed as

SymbiosisBase SequenceComputational BiologyEpichloeFungal ProteinsGreen Fluorescent ProteinsHyphaeImmunoprecipitationLoliumMicroscopy, ConfocalMicroscopy, Electron, TransmissionMolecular Sequence DataMultiprotein ComplexesNADPH OxidasesProtein Structure, TertiaryReactive Oxygen SpeciesFungal ProteinsGreen Fluorescent ProteinsMultiprotein ComplexesNADPH OxidasesReactive Oxygen Species

Identifiers

PMID21282602
PMCPMC3041104
OpenAlexW2085449098

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.