Evidence map›Paper›PMID 16864771›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties.

Thomas Boldog, Stephen Grimme, Mingshan Li, Stephen G Sligar, Gerald L Hazelbauer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

114 citing papers in PubMed, 190 citations in OpenAlex.

  1. A chemoreceptor conformational equilibrium controlled by signaling inputs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
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  8. Article
  9. Studying bacterial chemosensory array with CryoEM.Biochemical Society transactions · 2021
    Review
  10. Review
  11. Article
  12. Review
  13. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

54 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Thomas BoldogDepartment of Biochemistry, University of Missouri-Columbia, 117 Schweitzer Hall, Columbia, MO 65211, USA.
Stephen Grimme
Mingshan Li
Stephen G Sligar
Gerald L Hazelbauer
University of Missouri · USUniversity of Illinois Urbana-Champaign · US

Funding

Molecular Studies of Chemoreception: Administrative Supplement for EquipmentR37GM029963 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI HAZELBAUER, GERALD L. · 2012 to 2021
$5.7M
METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
MOLECULAR STUDIES OF CHEMORECEPTIONR01GM029963 · NIGMS · WASHINGTON STATE UNIVERSITY · PI HAZELBAUER, GERALD L. · 1985 to 2010
$4.2M
NIGMS NIH HHS GM29963NIGMS NIH HHS GM33775NIGMS NIH HHS R01 GM029963NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R37 GM029963
6 · The paper itself

Abstract

Bacterial chemoreceptors are transmembrane homodimers that can form trimers, higher order arrays, and extended clusters as part of signaling complexes. Interactions of dimers in oligomers are thought to confer cooperativity and cross-receptor influences as well as a 35-fold gain between ligand binding and altered kinase activity. In addition, higher order interactions among dimers are necessary for the observed patterns of assistance in adaptational modification among different receptors. Elucidating mechanisms underlying these properties will require defining which receptor functions can be performed by dimers and which require specific higher order interactions. However, such an assignment has not been possible. Here, we used Nanodiscs, an emerging technology for manipulating membrane proteins, to prepare small particles of lipid bilayer containing one or only a few chemoreceptor dimers. We found that receptor dimers isolated in individual Nanodiscs were readily modified, bound ligand, and performed transmembrane signaling. However, they were hardly able to activate the chemotaxis histidine kinase. Instead, maximal activation and thus full-range control of kinase occurred preferentially in discs containing approximately three chemoreceptor dimers. The sharp dependence of kinase activation on this number of receptors per dimer implies that the core structural unit of kinase activation and control is a trimer of dimers. Thus, our observations demonstrate that chemoreceptor transmembrane signaling does not require oligomeric organization beyond homodimers and implicate a trimer of dimers as the unit of downstream signaling.

Indexed as

Escherichia coli ProteinsMembrane ProteinsNanotechnologyProtein Structure, QuaternaryDimerizationEscherichia coliLipid BilayersModels, MolecularSignal TransductionEscherichia coli ProteinsLipid BilayersMembrane Proteins

Identifiers

PMID16864771
PMCPMC1544200
OpenAlexW2099134954

What OpenQuestion holds

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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.