Evidence map›Paper›PMID 25482645›Full record

ReviewCell adhesion & migration2014

Rho GTPase isoforms in cell motility: Don't fret, we have FRET.

Sara K Donnelly, Jose Javier Bravo-Cordero, Louis Hodgson

Open access · goldAbstract readReview
In one paragraph

Review in Cell adhesion & migration, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
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  8. Review
  9. Actin dynamics during tumor cell dissemination.International review of cell and molecular biology · 2021
    Review
  10. Frontiers in cell and developmental biology · 2021
    Review
  11. Textures of the tumour microenvironment.Essays in biochemistry · 2019
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Sara K Donnellya Department of Anatomy and Structural Biology ; Albert Einstein College of Medicine of Yeshiva University ; Bronx , NY USA.
Jose Javier Bravo-Cordero
Louis Hodgson
Albert Einstein College of Medicine · US

Funding

RhoC GTPase regulates leading edge protrusion dynamics in breast carcinomasR01GM093121 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI HODGSON, LOUIS · 2010 to 2014
$1.6M
NIGMS NIH HHS GM093121NIGMS NIH HHS R01 GM093121
6 · The paper itself

Abstract

The Rho-family of p21 small GTPases are directly linked to the regulation of actin-based motile machinery and play a key role in the control of cell migration. Aside from the original and most well-characterized canonical Rho GTPases RhoA, Rac1, and Cdc42, numerous isoforms of these key proteins have been identified and shown to have specific roles in regulating various cellular motility processes. The major difficulty in addressing these isoform-specific effects is that isoforms typically contain highly similar primary amino acid sequences and thus are able to interact with the same upstream regulators and the downstream effector targets. Here, we will introduce the major members of each GTPase subfamily and discuss recent advances in the design and application of fluorescent resonance energy transfer-based probes, which are at the forefront of the technologies available to directly probe the differential, spatiotemporal activation dynamics of these proteins in live single cells. Currently, it is possible to specifically detect the activation status of RhoA vs. RhoC isoforms, as well as Cdc42 vs. TC-10 isoforms in living cells. Clearly, additional efforts are still required to produce biosensor systems capable of detecting other isoforms of Rho GTPases including RhoB, Rac2/3, RhoG, etc. Through such efforts, we will uncover the isoform-specific roles of these near-identical proteins in living cells, clearly an important area of the Rho GTPase biology that is not yet fully appreciated.

Indexed as

Fluorescence Resonance Energy TransferActinsAmino Acid SequenceBiosensing TechniquesCell MovementHumansIsoenzymesrho GTP-Binding ProteinsActinsIsoenzymesrho GTP-Binding Proteins

Identifiers

PMID25482645
PMCPMC4594258
OpenAlexW2078638322

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.