Evidence map›Paper›PMID 28425142›Full record

ArticleProtein science : a publication of the Protein Society2017

Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation.

Wenlin Pan, Frederick W Dahlquist, Gerald L Hazelbauer

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
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  7. The structural logic of dynamic signaling in the Escherichia coli serine chemoreceptor.Protein science : a publication of the Protein Society · 2024
    Article
  8. The Structural Logic of Dynamic Signaling in thebioRxiv : the preprint server for biology · 2024
    Article
  9. Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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

3 authors at 2 institutions in 1 country.

Wenlin PanDepartment of Biochemistry, University of Missouri, Columbia, Missouri, 65211.
Frederick W DahlquistDepartment of Chemistry and Biochemistry and Department of Molecular, Cellular and Developmental Biology, University of California Santa Barbara, Santa Barbara, California, 93106-9510.
Gerald L HazelbauerDepartment of Biochemistry, University of Missouri, Columbia, Missouri, 65211.
University of Missouri · USUniversity of California, Santa Barbara · US

Funding

Molecular Studies of Chemoreception: Administrative Supplement for EquipmentR37GM029963 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI HAZELBAUER, GERALD L. · 2012 to 2021
$5.7M
MECHANISTIC STUDIES OF BACTERIAL CHEMOTAXISR01GM059544 · NIGMS · UNIVERSITY OF OREGON · PI DAHLQUIST, FREDERICK W. · 1999 to 2018
$4.8M
NIGMS NIH HHS R01 GM059544NIGMS NIH HHS R37 GM029963
6 · The paper itself

Abstract

Autophosphorylating histidine kinase CheA is central to signaling in bacterial chemotaxis. The kinase donates its phosphoryl group to two response regulators, CheY that controls flagellar rotation and thus motility and CheB, crucial for sensory adaptation. As measured by coupled CheY phosphorylation, incorporation into signaling complexes activates the kinase ∼1000-fold and places it under control of chemoreceptors. By the same assay, receptors modulate kinase activity ∼100-fold as a function of receptor ligand occupancy and adaptational modification. These changes are the essence of chemotactic signaling. Yet, the enzymatic properties affected by incorporation into signaling complexes, by chemoreceptor ligand binding or by receptor adaptational modification are largely undefined. To investigate, we performed steady-state kinetic analysis of autophosphorylation using a liberated kinase phosphoryl-accepting domain, characterizing kinase alone, in isolated core signaling complexes and in small arrays of core complexes assembled in vitro with receptors contained in isolated native membranes. Autophosphorylation in signaling complexes was measured as a function of ligand occupancy and adaptational modification. Activation by incorporation into signaling complexes and modulation in complexes by ligand occupancy and adaptational modification occurred largely via changes in the apparent catalytic rate constant (k

Indexed as

Amino Acid MotifsAspartic AcidBacterial ProteinsBinding SitesChemotaxisEscherichia coliEscherichia coli ProteinsGene ExpressionHistidine KinaseKineticsLigandsMethyl-Accepting Chemotaxis ProteinsPhosphorylationProtein BindingProtein DomainsProtein MultimerizationAspartic AcidBacterial ProteinscheA protein, E coliCheB protein, BacteriacheY protein, E coliEscherichia coli ProteinsHistidine KinaseLigandsMethyl-Accepting Chemotaxis ProteinsReceptors, Cell SurfaceRecombinant ProteinsTar protein, E colibacterial chemoreceptorsbacterial chemotaxisenzyme kineticshistidine kinaseNanodiscs

Identifiers

PMID28425142
PMCPMC5521549
OpenAlexW2607429622

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.