Evidence map›Paper›PMID 18430134›Full record

ArticleMolecular microbiology2008

The receiver domain of FrzE, a CheA-CheY fusion protein, regulates the CheA histidine kinase activity and downstream signalling to the A- and S-motility systems of Myxococcus xanthus.

Yuki F Inclán, Sophie Laurent, David R Zusman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Milestones in the development ofJournal of bacteriology · 2025
    Review
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  20. Developments in Defining dif.Journal of bacteriology · 2010
    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 2 institutions in 1 country.

Yuki F InclánUniversity of California, Graduate Group in Biophysics, Berkeley, CA 94720-3204, USA.
Sophie Laurent
David R Zusman
Molecular Sciences Institute · USUniversity of California, Berkeley · US

Funding

SENSORY TRANSDUCTION AND DEVELOPMENT IN A BACTERIUMR01GM020509 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZUSMAN, DAVID ROBERT · 1985 to 2014
$5.9M
NIGMS NIH HHS GM20509NIGMS NIH HHS R01 GM020509
6 · The paper itself

Abstract

The Frz chemosensory system is a two-component signal transduction pathway that controls cell reversals and directional movements for the two motility systems in Myxococcus xanthus. To trigger cell reversals, FrzE, a hybrid CheA-CheY fusion protein, autophosphorylates the kinase domain at His-49, and phosphoryl groups are transferred to aspartate residues (Asp-52 and Asp-220) in the two receiver domains of FrzZ, a dual CheY-like protein that serves as the pathway output. The role of the receiver domain of FrzE was unknown. In this paper, we characterize the FrzE protein in vitro and show that the receiver domain of FrzE negatively regulates the autophosphorylation activity of the kinase domain of FrzE. Unexpectedly, it does not appear to play a direct role in phospho-relay as in most other histidine kinase receiver domain hybrid systems. The regulatory role of the FrzE receiver domain suggests that it may interact with or be phosphorylated by an unknown protein. We also show the dynamics of motility system-specific marker proteins in FrzE mutants as cells move forward and reverse. Our studies indicate that the two motility systems are functionally co-ordinated and that any system-specific branching of the pathway most likely occurs downstream of FrzE.

Indexed as

Cell MovementSignal TransductionBacterial ProteinsChemotaxisGene Expression Regulation, BacterialHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMyxococcus xanthusProtein KinasesRecombinant Fusion ProteinsBacterial ProteinsFrzZ protein, Myxococcus xanthusHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsProtein KinasesRecombinant Fusion Proteins

Identifiers

PMID18430134
PMCPMC2830897
OpenAlexW2067188262

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.