Evidence map›Paper›PMID 22226748›Full record

ArticleCurrent biology : CB2012

The RhoGAP domain of CYK-4 has an essential role in RhoA activation.

Andy Loria, Katrina M Longhini, Michael Glotzer

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Mitotic Cell Division inGenetics · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Cytokinesis in Metazoa and Fungi.Cold Spring Harbor perspectives in biology · 2017
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Andy LoriaDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA.
Katrina M Longhini
Michael Glotzer
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
PREDOCTORAL TRAINING IN GENETICS AND REGULATIONT32GM007197 · NIGMS · UNIVERSITY OF CHICAGO · PI ROTHMAN-DENES, LUCIA B. B · 1985 to 2020
$17.0M
Positioning the Plane of Cell Division During CytokinesisR01GM085087 · NIGMS · UNIVERSITY OF CHICAGO · PI GLOTZER, MICHAEL A. · 2008 to 2018
$3.3M
Molecular Dissection of CytokinesisR01GM074743 · NIGMS · UNIVERSITY OF CHICAGO · PI GLOTZER, MICHAEL A. · 2006 to 2009
$1.1M
NIGMS NIH HHS R01 GM074743NIGMS NIH HHS R01 GM085087NIGMS NIH HHS R01 GM74743NIGMS NIH HHS T32 GM007183NIGMS NIH HHS T32 GM007197
6 · The paper itself

Abstract

Cytokinesis in animal cells is mediated by a cortical actomyosin-based contractile ring. The GTPase RhoA is a critical regulator of this process as it activates both nonmuscle myosin and a nucleator of actin filaments [1]. The site at which active RhoA and its effectors accumulate is controlled by the microtubule-based spindle during anaphase [2]. ECT-2, the guanine nucleotide exchange factor (GEF) that activates RhoA during cytokinesis, is regulated by phosphorylation and subcellular localization [3-5]. ECT2 localization depends on interactions with CYK-4/MgcRacGAP, a Rho GTPase-activating protein (GAP) domain containing protein [5, 6]. Here we show that, contrary to expectations, the Rho GTPase-activating protein (GAP) domain of CYK-4 promotes activation of RhoA during cytokinesis. Furthermore, we show that the primary phenotype caused by mutations in the GAP domain of CYK-4 is not caused by ectopic activation of CED-10/Rac1 and ARX-2/Arp2. However, inhibition of CED-10/Rac1 and ARX-2/Arp2 facilitates ingression of weak cleavage furrows. These results demonstrate that a GAP domain can contribute to activation of a small GTPase. Furthermore, cleavage furrow ingression is sensitive to the balance of contractile forces and cortical tension.

Indexed as

Actin-Related Protein 2AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCytokinesisEmbryo, NonmammalianProtein Structure, Tertiaryrac GTP-Binding ProteinsrhoA GTP-Binding ProteinActin-Related Protein 2arx-2 protein, C elegansCaenorhabditis elegans ProteinsCED-10 protein, C elegansCYK-4 protein, C elegansrac GTP-Binding ProteinsrhoA GTP-Binding Protein

Identifiers

PMID22226748
PMCPMC3285270
OpenAlexW2095110680

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.