Evidence map›Paper›PMID 18711126›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Receptor density balances signal stimulation and attenuation in membrane-assembled complexes of bacterial chemotaxis signaling proteins.

Tatiana Y Besschetnova, David J Montefusco, Abdalin E Asinas, Anthony L Shrout, Frances M Antommattei, Robert M Weis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. 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
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  8. ProBLM web server: protein and membrane placement and orientation package.Computational and mathematical methods in medicine · 2014
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  14. A dynamic-signaling-team model for chemotaxis receptors in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2010
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  15. Review
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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

6 authors at 1 institution in 1 country.

Tatiana Y BesschetnovaDepartment of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003-9336, USA.
David J Montefusco
Abdalin E Asinas
Anthony L Shrout
Frances M Antommattei
Robert M Weis
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
LIGAND &SUBUNIT INTERACTIONS OF TRANSMEMBRANE RECEPTORSR01GM053210 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI WEIS, ROBERT M · 1997 to 2004
$812k
NIGMS NIH HHS 5T32GM008515NIGMS NIH HHS R01 GM053210NIGMS NIH HHS R01 GM53210NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

All cells possess transmembrane signaling systems that function in the environment of the lipid bilayer. In the Escherichia coli chemotaxis pathway, the binding of attractants to a two-dimensional array of receptors and signaling proteins simultaneously inhibits an associated kinase and stimulates receptor methylation--a slower process that restores kinase activity. These two opposing effects lead to robust adaptation toward stimuli through a physical mechanism that is not understood. Here, we provide evidence of a counterbalancing influence exerted by receptor density on kinase stimulation and receptor methylation. Receptor signaling complexes were reconstituted over a range of defined surface concentrations by using a template-directed assembly method, and the kinase and receptor methylation activities were measured. Kinase activity and methylation rates were both found to vary significantly with surface concentration--yet in opposite ways: samples prepared at high surface densities stimulated kinase activity more effectively than low-density samples, whereas lower surface densities produced greater methylation rates than higher densities. FRET experiments demonstrated that the cooperative change in kinase activity coincided with a change in the arrangement of the membrane-associated receptor domains. The counterbalancing influence of density on receptor methylation and kinase stimulation leads naturally to a model for signal regulation that is compatible with the known logic of the E. coli pathway. Density-dependent mechanisms are likely to be general and may operate when two or more membrane-related processes are influenced differently by the two-dimensional concentration of pathway elements.

Indexed as

ChemotaxisMultiprotein ComplexesReceptors, Cell SurfaceSignal TransductionBacterial ProteinsEscherichia coliEscherichia coli ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMethylationProtein KinasesBacterial ProteinsCheW protein, E coliEscherichia coli ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMultiprotein ComplexesProtein KinasesReceptors, Cell Surface

Identifiers

PMID18711126
PMCPMC2527904
OpenAlexW1977110567

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.