Evidence map›Paper›PMID 22916026›Full record

ArticlePLoS genetics2012

A dynamic response regulator protein modulates G-protein-dependent polarity in the bacterium Myxococcus xanthus.

Yong Zhang, Mathilde Guzzo, Adrien Ducret, Yue-Zhong Li, Tâm Mignot

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 65 citations in OpenAlex.

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  12. Microorganisms · 2021
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  13. Linking single-cell decisions to collective behaviours in social bacteria.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
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  14. The polar Ras-like GTPase MglA activates type IV pilus via SgmX to enable twitching motility inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Establishing rod shape from spherical, peptidoglycan-deficient bacterial spores.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 3 institutions in 2 countries.

Yong ZhangLaboratoire de Chimie Bactérienne, CNRS UPR9043, Institut de Microbiologie de la Méditerranée, Université Aix-Marseille, Marseille, France.
Mathilde Guzzo
Adrien Ducret
Yue-Zhong Li
Tâm Mignot
Centre National de la Recherche Scientifique · FRLaboratoire de Chimie Bactérienne · FRState Key Laboratory of Microbial Technology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Migrating cells employ sophisticated signal transduction systems to respond to their environment and polarize towards attractant sources. Bacterial cells also regulate their polarity dynamically to reverse their direction of movement. In Myxococcus xanthus, a GTP-bound Ras-like G-protein, MglA, activates the motility machineries at the leading cell pole. Reversals are provoked by pole-to-pole switching of MglA, which is under the control of a chemosensory-like signal transduction cascade (Frz). It was previously known that the asymmetric localization of MglA at one cell pole is regulated by MglB, a GTPase Activating Protein (GAP). In this process, MglB specifically localizes at the opposite lagging cell pole and blocks MglA localization at that pole. However, how MglA is targeted to the leading pole and how Frz activity switches the localizations of MglA and MglB synchronously remained unknown. Here, we show that MglA requires RomR, a previously known response regulator protein, to localize to the leading cell pole efficiently. Specifically, RomR-MglA and RomR-MglB complexes are formed and act complementarily to establish the polarity axis, segregating MglA and MglB to opposite cell poles. Finally, we present evidence that Frz signaling may regulate MglA localization through RomR, suggesting that RomR constitutes a link between the Frz-signaling and MglAB polarity modules. Thus, in Myxococcus xanthus, a response regulator protein governs the localization of a small G-protein, adding further insight to the polarization mechanism and suggesting that motility regulation evolved by recruiting and combining existing signaling modules of diverse origins.

Indexed as

Bacterial ProteinsCell PolarityChemotaxisGTPase-Activating ProteinsGuanosine TriphosphateMyxococcus xanthusProtein BindingSignal TransductionBacterial ProteinsFrzZ protein, Myxococcus xanthusGTPase-Activating ProteinsGuanosine TriphosphateMglA protein, Myxococcus xanthus

Identifiers

PMID22916026
PMCPMC3420945
OpenAlexW2009386800

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.