Evidence map›Paper›PMID 23543749›Full record

ArticleThe Journal of biological chemistry2013

Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase.

Deniz B Temel, Kaushik Dutta, Sébastien Alphonse, Julien Nourikyan, Christophe Grangeasse, Ranajeet Ghose

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Axenic Biofilm Formation and Aggregation byApplied and environmental microbiology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Microbial protein-tyrosine kinases.The Journal of biological chemistry · 2014
    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

6 authors at 4 institutions in 2 countries.

Deniz B TemelDepartment of Chemistry, City College of New York, New York, New York 10031, USA.
Kaushik Dutta
Sébastien Alphonse
Julien Nourikyan
Christophe Grangeasse
Ranajeet Ghose
City College of New York · USCity University of New York · USCentre National de la Recherche Scientifique · FRNew York Structural Biology Center · US

Funding

TNC FUNCTION IN APOPTOTIC ANTIGEN DRIVEN AUTOIMMUNITYG12RR003060 · NCRR · CITY COLLEGE OF NEW YORK · PI GUYDEN, JERRY · 1985 to 2011
$26.1M
Cellular/Molecular Basis of Development: Research CenterG12MD007603 · NIMHD · CITY COLLEGE OF NEW YORK · PI PEZZANO, MARK · 2012 to 2017
$11.5M
900 MHz NMR Spectrometer for Structural BiologyP41GM066354 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI COWBURN, DAVID · 2002 to 2006
$4.7M
EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR015495 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI RIFKIND, RICHARD A · 2000 to 2000
$2.0M
Catalytic Domain Dynamics in Protein KinasesR01GM084278 · NIGMS · CITY COLLEGE OF NEW YORK · PI GHOSE, RANAJEET · 2009 to 2013
$1.6M
Interactions between Bacterial Tyrosine Kinases and PhosphatasesR21AI101792 · NIAID · CITY COLLEGE OF NEW YORK · PI GHOSE, RANAJEET · 2012 to 2013
$429k
NCI NIH HHS CO6RR015495NCRR NIH HHS 2G12RR03060NCRR NIH HHS C06 RR015495NCRR NIH HHS G12 RR003060NIAID NIH HHS AI101792NIAID NIH HHS R21 AI101792NIGMS NIH HHS GM084278NIGMS NIH HHS P41 GM066354NIGMS NIH HHS P41GM066354NIGMS NIH HHS R01 GM084278NIMHD NIH HHS 8G12MD007603NIMHD NIH HHS G12 MD007603
6 · The paper itself

Abstract

The cyclic process of autophosphorylation of the C-terminal tyrosine cluster (YC) of a bacterial tyrosine kinase and its subsequent dephosphorylation following interactions with a counteracting tyrosine phosphatase regulates diverse physiological processes, including the biosynthesis and export of polysaccharides responsible for the formation of biofilms or virulence-determining capsules. We provide here the first detailed insight into this hitherto uncharacterized regulatory interaction at residue-specific resolution using Escherichia coli Wzc, a canonical bacterial tyrosine kinase, and its opposing tyrosine phosphatase, Wzb. The phosphatase Wzb utilizes a surface distal to the catalytic elements of the kinase, Wzc, to dock onto its catalytic domain (WzcCD). WzcCD binds in a largely YC-independent fashion near the Wzb catalytic site, inducing allosteric changes therein. YC dephosphorylation is proximity-mediated and reliant on the elevated concentration of phosphorylated YC near the Wzb active site resulting from WzcCD docking. Wzb principally recognizes the phosphate of its phosphotyrosine substrate and further stabilizes the tyrosine moiety through ring stacking interactions with a conserved active site tyrosine.

Indexed as

Allosteric RegulationCatalytic DomainEscherichia coliEscherichia coli ProteinsMembrane ProteinsPhosphoprotein PhosphatasesPhosphotyrosineProtein-Tyrosine KinasesEscherichia coli ProteinsMembrane ProteinsPhosphoprotein PhosphatasesPhosphotyrosineProtein-Tyrosine KinasesWzb protein, E coliwzc protein, E coliNMRProkaryotic Signal TransductionProtein-Protein InteractionsProtein-tyrosine Kinase (Tyrosine Kinase)Protein-tyrosine Phosphatase (Tyrosine Phosphatase)

Identifiers

PMID23543749
PMCPMC3663541
OpenAlexW1967995546

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.