Evidence map›Paper›PMID 28001128›Full record

ArticleeLife2016

Coincidence detection and bi-directional transmembrane signaling control a bacterial second messenger receptor.

Richard B Cooley, John P O'Donnell, Holger Sondermann

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. UnderstandingMicroorganisms · 2026
    Review
  3. Reconstitution of a biofilm adhesin system from a sulfate-reducing bacterium inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. CdgC, a Cyclic-di-GMP Diguanylate Cyclase ofFrontiers in plant science · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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 1 institution in 1 country.

Richard B CooleyDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, United States.
John P O'DonnellDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, United States.
Holger SondermannDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, United States.ORCID 0000-0003-2211-6234
Cornell University · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
CHEMISTRY OF BIOLOGICAL SYSTEMST32GM008500 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIN, HENING · 1996 to 2020
$5.4M
Molecular mechanism regulating periplasmic proteolysis in bacterial pathogenesisR01AI097307 · NIAID · CORNELL UNIVERSITY · PI O'TOOLE, GEORGE A., SONDERMANN, HOLGER · 2012 to 2016
$1.9M
Mechanism and function of a conserved bacterial cyclic-di-GMP receptor systemF32GM108440 · NIGMS · CORNELL UNIVERSITY · PI COOLEY, RICHARD B · 2013 to 2014
$102k
NIAID NIH HHS R01 AI097307NIGMS NIH HHS F32 GM108440NIGMS NIH HHS P41 GM103485NIGMS NIH HHS T32 GM008500
6 · The paper itself

Abstract

The second messenger c-di-GMP (or cyclic diguanylate) regulates biofilm formation, a physiological adaptation process in bacteria, via a widely conserved signaling node comprising a prototypical transmembrane receptor for c-di-GMP, LapD, and a cognate periplasmic protease, LapG. Previously, we reported a structure-function study of a soluble LapD•LapG complex, which established conformational changes in the receptor that lead to c-di-GMP-dependent protease recruitment (Chatterjee et al., 2014). This work also revealed a basal affinity of c-di-GMP-unbound receptor for LapG, the relevance of which remained enigmatic. Here, we elucidate the structural basis of coincidence detection that relies on both c-di-GMP and LapG binding to LapD for receptor activation. The data indicate that high-affinity for LapG relies on the formation of a receptor dimer-of-dimers, rather than a simple conformational change within dimeric LapD. The proposed mechanism provides a rationale of how external proteins can regulate receptor function and may also apply to c-di-GMP-metabolizing enzymes that are akin to LapD.

Indexed as

Second Messenger SystemsSignal TransductionBacterial ProteinsCyclic GMPModels, BiologicalProtein ConformationProtein MultimerizationPseudomonas fluorescensScattering, Small AngleBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPbiofilm formationbiophysicsinfectious diseasemembrane protein structuremembrane signalingmicrobiologysecond messengerstructural biology

Identifiers

PMID28001128
PMCPMC5231407
OpenAlexW2563523543

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.