Evidence map›Paper›PMID 33853736›Full record

ReviewTrends in microbiology2021

A Radical Reimagining of Fungal Two-Component Regulatory Systems.

Robert B Bourret, Emily N Kennedy, Clay A Foster, Victoria E Sepúlveda, William E Goldman

Abstract readReview
In one paragraph

Review in Trends in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Real-time detection of response regulator phosphorylation dynamics in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. 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

5 authors.

Robert B BourretDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, NC 27599-7290, USA. Electronic address: bourret@med.unc.edu.
Emily N KennedyDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, NC 27599-7290, USA.
Clay A FosterDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, NC 27599-7290, USA.
Victoria E SepúlvedaDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, NC 27599-7290, USA.
William E GoldmanDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, NC 27599-7290, USA.

Funding

Molecular Mechanisms of Signal Transduction by Two-Component Regulatory SystemsR01GM050860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BOURRET, ROBERT B. · 1994 to 2025
$7.9M
The evolution of virulence in the fungal pathogen HistoplasmaR01AI153523 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MATUTE, DANIEL · 2021 to 2025
$3.2M
NIAID NIH HHS R01 AI153523NIGMS NIH HHS R01 GM050860
6 · The paper itself

Abstract

Bacterial two-component regulatory systems (TCSs) mediate signal transduction by transferring phosphoryl groups between sensor kinase and response regulator proteins, sometimes using intermediary histidine-phosphotransferase (Hpt) domains to form multistep phosphorelays. Because (i) almost all known fungal sensor kinases exhibit a domain architecture characteristic of bacterial TCS phosphorelays, (ii) all known fungal Hpts are stand-alone proteins suited to shuttle between cytoplasm and nucleus, and (iii) the best-characterized fungal TCS is a canonical phosphorelay, it is widely assumed that most or all fungal TCSs function via phosphorelays. However, fungi generally encode more sensor kinases than Hpts or response regulators, leading to a disparity between putative phosphorelay inputs and outputs. The simplest resolution of this paradox is to hypothesize that most fungal sensor kinases do not participate in phosphorelays. Reimagining how fungal TCSs might function leads to multiple testable predictions.

Indexed as

Gene Expression Regulation, FungalFungal ProteinsFungiHistidine KinaseSignal TransductionFungal ProteinsHistidine Kinasefungihistidine-containing phosphotransfer proteinhybrid histidine kinasephosphorelayresponse regulatortwo-component regulatory systems

Identifiers

PMID33853736
PMCPMC8440447

What OpenQuestion holds

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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.