Evidence map›Paper›PMID 24347630›Full record

ArticleG3 (Bethesda, Md.)2014

Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase.

Arit Ghosh, Jacqueline A Servin, Gyungsoon Park, Katherine A Borkovich

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2014. 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
2.3field-weighted citation impact, top 14% 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, 45 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Arit GhoshDepartment of Plant Pathology and Microbiology, University of California, Riverside, California 92521.
Jacqueline A Servin
Gyungsoon Park
Katherine A Borkovich
University of California, Riverside · US

Funding

Tools for Functional Analysis and Cell BiologyP01GM068087 · NIGMS · DARTMOUTH COLLEGE · PI DUNLAP, JAY C. · 2004 to 2013
$19.3M
NIGMS NIH HHS P01 GM068087NIGMS NIH HHS P01GM068087
6 · The paper itself

Abstract

Protein phosphatases are integral components of the cellular signaling machinery in eukaryotes, regulating diverse aspects of growth and development. The genome of the filamentous fungus and model organism Neurospora crassa encodes catalytic subunits for 30 protein phosphatase genes. In this study, we have characterized 24 viable N. crassa phosphatase catalytic subunit knockout mutants for phenotypes during growth, asexual development, and sexual development. We found that 91% of the mutants had defects in at least one of these traits, whereas 29% possessed phenotypes in all three. Chemical sensitivity screens were conducted to reveal additional phenotypes for the mutants. This resulted in the identification of at least one chemical sensitivity phenotype for 17 phosphatase knockout mutants, including novel chemical sensitivities for two phosphatase mutants lacking a growth or developmental phenotype. Hence, chemical sensitivity or growth/developmental phenotype was observed for all 24 viable mutants. We investigated p38 mitogen-activated protein kinase (MAPK) phosphorylation profiles in the phosphatase mutants and identified nine potential candidates for regulators of the p38 MAPK. We demonstrated that the PP2C class phosphatase pph-8 (NCU04600) is an important regulator of female sexual development in N. crassa. In addition, we showed that the Δcsp-6 (ΔNCU08380) mutant exhibits a phenotype similar to the previously identified conidial separation mutants, Δcsp-1 and Δcsp-2, that lack transcription factors important for regulation of conidiation and the circadian clock.

Indexed as

Genome, FungalCatalytic DomainFungal ProteinsMutationNeurospora crassap38 Mitogen-Activated Protein KinasesPhenotypePhosphoprotein PhosphatasesProtein Tyrosine PhosphatasesSpores, FungalFungal Proteinsp38 Mitogen-Activated Protein KinasesPhosphoprotein PhosphatasesProtein Tyrosine Phosphatasesfilamentous fungifunctional genomicsprotein phosphorylationserine-threonine protein phosphatasestyrosine protein phosphatases

Identifiers

PMID24347630
PMCPMC3931568
OpenAlexW1965153117

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.