Evidence map›Paper›PMID 23932593›Full record

ArticleStructure (London, England : 1993)2013

Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein.

Jimmy A Blair, Qingping Xu, W Seth Childers, Irimpan I Mathews, Justin W Kern, Michael Eckart, Ashley M Deacon, Lucy Shapiro

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Integration of cell cycle signals by multi-PAS domain kinases.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. 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

8 authors at 2 institutions in 1 country.

Jimmy A BlairDepartment of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Qingping Xu
W Seth Childers
Irimpan I Mathews
Justin W Kern
Michael Eckart
Ashley M Deacon
Lucy Shapiro
Stanford University · USSLAC National Accelerator Laboratory · US

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2005 to 2009
$50.6M
Structure Determination Core at SSRLU54GM094586 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2010 to 2014
$40.1M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
REGULATION OF DIFFERENTIATION IN CAULOBACTERR01GM032506 · NIGMS · YESHIVA UNIVERSITY · PI SHAPIRO, LUCILLE · 1985 to 2014
$7.1M
DEVELOPMENT CONTROL OF DNA REPLICATION IN CAULOBACTERR01GM051426 · NIGMS · STANFORD UNIVERSITY · PI SHAPIRO, LUCILLE · 1994 to 2013
$3.8M
Membrane protein localization and function in Caulobacter cytokinesisF32GM099173 · NIGMS · STANFORD UNIVERSITY · PI KERN, JUSTIN · 2011 to 2012
$101k
NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIGMS NIH HHS F32 GM099173NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM032506NIGMS NIH HHS R01 GM051426NIGMS NIH HHS R01 GM32506NIGMS NIH HHS R01 GM51426NIGMS NIH HHS U54 GM074898NIGMS NIH HHS U54 GM094586PHS HHS F32 A1082915
6 · The paper itself

Abstract

Vital to bacterial survival is the faithful propagation of cellular signals, and in Caulobacter crescentus, ChpT is an essential mediator within the cell-cycle circuit. ChpT functions as a histidine-containing phosphotransfer protein (HPt) that shuttles a phosphoryl group from the receiver domain of CckA, the upstream hybrid histidine kinase (HK), to one of two downstream response regulators (CtrA or CpdR) that controls cell-cycle progression. To understand how ChpT interacts with multiple signaling partners, we solved the crystal structure of ChpT at 2.3 Å resolution. ChpT adopts a pseudo-HK architecture but does not bind ATP. We identified two point mutation classes affecting phosphotransfer and cell morphology: one that globally impairs ChpT phosphotransfer, and a second that mediates partner selection. Importantly, a small set of conserved ChpT residues promotes signaling crosstalk and contributes to the branched signaling that activates the master regulator CtrA while inactivating the CtrA degradation signal, CpdR.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsCaulobacter crescentusConserved SequenceCrystallography, X-RayHydrolysisKineticsModels, MolecularMolecular Sequence DataPhosphorylationPoint MutationProtein BindingProtein Processing, Post-TranslationalProtein Structure, SecondaryAdenosine TriphosphateBacterial ProteinsTransferases

Identifiers

PMID23932593
PMCPMC3787845
OpenAlexW2007119688

What OpenQuestion holds

Textmetadata
LicenceTDM
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.