Evidence map›Paper›PMID 34633047›Full record

ArticleJournal of cell science2021

Dia- and Rok-dependent enrichment of capping proteins in a cortical region.

Anja Schmidt, Long Li, Zhiyi Lv, Shuling Yan, Jörg Großhans

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Actomyosin contraction in the follicular epithelium provides the major mechanical force for follicle rupture duringProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. 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 2 institutions in 2 countries.

Anja SchmidtDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Long LiDepartment of Biology/FB17, Philipps University, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.
Zhiyi LvDepartment of Biology/FB17, Philipps University, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.
Shuling YanDepartment of Biology/FB17, Philipps University, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.
Jörg GroßhansDepartment of Biology/FB17, Philipps University, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.ORCID 0000-0003-1114-9233
Philipps University of Marburg · DEUniversity of North Carolina at Chapel Hill · US

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
NIH HHS P40 OD018537
6 · The paper itself

Abstract

Rho signaling with its major targets the formin Dia, Rho kinase (Rok) and non-muscle myosin II (MyoII, encoded by zip in flies) control turnover, amount and contractility of actomyosin. Much less investigated has been a potential function for the distribution of F-actin plus and minus ends. In syncytial Drosophila embryos, Rho1 signaling is high between actin caps, i.e. the cortical intercap region. Capping protein binds to free plus ends of F-actin to prevent elongation of the filament. Capping protein has served as a marker to visualize the distribution of F-actin plus ends in cells and in vitro. In the present study, we probed the distribution of plus ends with capping protein in syncytial Drosophila embryos. We found that capping proteins are specifically enriched in the intercap region similar to Dia and MyoII but distinct from overall F-actin. The intercap enrichment of Capping protein was impaired in dia mutants and embryos, in which Rok and MyoII activation was inhibited. Our observations reveal that Dia and Rok-MyoII control Capping protein enrichment and support a model that Dia and Rok-MyoII control the organization of cortical actin cytoskeleton downstream of Rho1 signaling. This article has an associated First Person interview with the first authors of the paper.

Indexed as

Drosophila ProteinsForminsrho-Associated KinasesActin CytoskeletonActinsAnimalsDrosophilaMembrane ProteinsMyosin Heavy ChainsActinsdiaphanous protein, DrosophilaDrosophila ProteinsForminsMembrane ProteinsMyosin Heavy Chainsrho-Associated KinasesZip protein, DrosophilaActinCapping proteinCell cortexDiaDrosophilaEmbryoEpithelial domainForminMyosinSubapical

Identifiers

PMID34633047
PMCPMC8627554
OpenAlexW3207603839

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.