Evidence map›Paper›PMID 27009206›Full record

ArticleMolecular biology of the cell2016

The novel RacE-binding protein GflB sharpens Ras activity at the leading edge of migrating cells.

Hiroshi Senoo, Huaqing Cai, Yu Wang, Hiromi Sesaki, Miho Iijima

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Functional integrity of the contractile actin cortex is safeguarded by multiple Diaphanous-related formins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Mutually inhibitory Ras-PI(3,4)PProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. 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

5 authors at 1 institution in 2 countries.

Hiroshi SenooDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Huaqing CaiDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205 State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Yu WangDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Hiromi SesakiDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Miho IijimaDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205 miijima@jhmi.edu.
Johns Hopkins University · US

Funding

Lipid Signaling in ChemotaxisR01GM084015 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI IIJIMA, MIHO · 2009 to 2019
$2.9M
Mitochondrial Fusion and DivisionR01GM089853 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SESAKI, HIROMI · 2010 to 2014
$2.1M
NIGMS NIH HHS R01 GM084015NIGMS NIH HHS R01 GM089853
6 · The paper itself

Abstract

Directional sensing, a process in which cells convert an external chemical gradient into internal signaling events, is essential in chemotaxis. We previously showed that a Rho GTPase, RacE, regulates gradient sensing in Dictyostelium cells. Here, using affinity purification and mass spectrometry, we identify a novel RacE-binding protein, GflB, which contains a Ras GEF domain and a Rho GAP domain. Using biochemical and gene knockout approaches, we show that GflB balances the activation of Ras and Rho GTPases, which enables cells to precisely orient signaling events toward higher concentrations of chemoattractants. Furthermore, we find that GflB is located at the leading edge of migrating cells, and this localization is regulated by the actin cytoskeleton and phosphatidylserine. Our findings provide a new molecular mechanism that connects directional sensing and morphological polarization.

Indexed as

Carrier ProteinsCell MovementChemotaxisCyclic AMPDictyosteliumGTPase-Activating ProteinsProtein BindingProtein DomainsProtozoan Proteinsras Proteinsrho GTP-Binding ProteinsSignal TransductionCarrier ProteinsCyclic AMPGTPase-Activating ProteinsProtozoan Proteinsras Proteinsrho GTPase-activating proteinrho GTP-Binding Proteins

Identifiers

PMID27009206
PMCPMC4865317
OpenAlexW2317306551

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.