Evidence map›Paper›PMID 31171861›Full record

ArticleScientific reports2019

Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division.

Iswahyudi, Galina V Mukamolova, Anna A Straatman-Iwanowska, Natalie Allcock, Paul Ajuh, Obolbek Turapov, Helen M O'Hare

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-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

17 citing papers in PubMed, 25 citations in OpenAlex.

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  10. An Epistatic Network DescribesFrontiers in molecular biosciences · 2022
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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

7 authors at 2 institutions in 2 countries.

IswahyudiLeicester TB Research Group, Department of Respiratory Sciences, University of Leicester, LE1 7RH, Leicester, UK.
Galina V MukamolovaLeicester TB Research Group, Department of Respiratory Sciences, University of Leicester, LE1 7RH, Leicester, UK.ORCID http://orcid.org/0000-0001-5697-2018
Anna A Straatman-IwanowskaLeicester Core Biotechnology Services Electron Microscopy Facility, University of Leicester, Leicester, UK.
Natalie AllcockLeicester Core Biotechnology Services Electron Microscopy Facility, University of Leicester, Leicester, UK.
Paul AjuhGemini Biosciences Ltd, Liverpool Science Park, Liverpool, United Kingdom.
Obolbek TurapovLeicester TB Research Group, Department of Respiratory Sciences, University of Leicester, LE1 7RH, Leicester, UK.
Helen M O'HareLeicester TB Research Group, Department of Respiratory Sciences, University of Leicester, LE1 7RH, Leicester, UK. hmo7@le.ac.uk.
University of Leicester · GBTanjungpura University · ID

Funding

Biotechnology and Biological Sciences Research Council BB/P001513/1
6 · The paper itself

Abstract

Protein phosphatase PstP is conserved throughout the Actinobacteria in a genetic locus related to cell wall synthesis and cell division. In many Actinobacteria it is the sole annotated serine threonine protein phosphatase to counter the activity of multiple serine threonine protein kinases. We used transcriptional knockdown, electron microscopy and comparative phosphoproteomics to investigate the putative dual functions of PstP as a specific regulator of cell division and as a global regulator of protein phosphorylation. Comparative phosphoproteomics in the early stages of PstP depletion showed hyperphosphorylation of protein kinases and their substrates, confirming PstP as a negative regulator of kinase activity and global serine and threonine phosphorylation. Analysis of the 838 phosphorylation sites that changed significantly, suggested that PstP may regulate diverse phosphoproteins, preferentially at phosphothreonine near acidic residues, near the protein termini, and within membrane associated proteins. Increased phosphorylation of the activation loop of protein kinase B (PknB) and of the essential PknB substrate CwlM offer possible explanations for the requirement for pstP for growth and for cell wall defects when PstP was depleted.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsCell WallComputer SimulationMicroscopy, ElectronMultigene FamilyMutationMycobacterium smegmatisMycobacterium tuberculosisPhosphoproteinsPhosphorylationPromoter Regions, GeneticProtein Serine-Threonine KinasesProteomicsBacterial ProteinsPhosphoproteinsPknB protein, Mycobacterium tuberculosisProtein Serine-Threonine Kinases

Identifiers

PMID31171861
PMCPMC6554272
OpenAlexW2948620322

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.