Evidence map›Paper›PMID 25589578›Full record

ArticleOpen biology2015

Drosophila gene tao-1 encodes proteins with and without a Ste20 kinase domain that affect cytoskeletal architecture and cell migration differently.

Ralf Pflanz, Aaron Voigt, Toma Yakulov, Herbert Jäckle

Abstract read
In one paragraph

Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

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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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The Diverse Roles of TAO Kinases in Health and Diseases.International journal of molecular sciences · 2020
    Review
  6. Conserved Tao Kinase Activity Regulates Dendritic Arborization, Cytoskeletal Dynamics, and Sensory Function inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  7. Article
  8. Review
  9. 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

4 authors.

Ralf PflanzAbteilung Molekulare Entwicklungsbiologie, Max Planck Institut für Biophysikalische Chemie, Göttingen, Germany.
Aaron VoigtAbteilung Molekulare Entwicklungsbiologie, Max Planck Institut für Biophysikalische Chemie, Göttingen, Germany Department of Neurology, University Medical Centre Aachen, Aachen, Germany.
Toma YakulovAbteilung Molekulare Entwicklungsbiologie, Max Planck Institut für Biophysikalische Chemie, Göttingen, Germany Renal Division, University Hospital Freiburg, Freiburg, Germany.
Herbert JäckleAbteilung Molekulare Entwicklungsbiologie, Max Planck Institut für Biophysikalische Chemie, Göttingen, Germany hjaeckl@gwdg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tao-1, the single representative of the Sterile 20 kinase subfamily in Drosophila, is best known for destabilizing microtubules at the actin-rich cortex, regulating the cytoskeletal architecture of cells. More recently, Tao-1 was shown to act in the Salvador-Warts-Hippo pathway by phosphorylating Hippo, regulating cell growth as well as cell polarity. Here, we show that tao-1 encodes two proteins, one with the Sterile 20 kinase domain (Tao-L) and one without it (Tao-S), and that they act in an antagonistic manner. Tao-L expression causes lamellipodia-like cell protrusions, whereas Tao-S expression results in filopodia-like structures that make cells stick to the surface they attach to. Ectopic Tao-1 expression in the anterior region of Drosophila embryos results in pole cell formation as normally observed at the posterior end. Tao-S expression causes primordial germ cells (PGCs) to adhere to the inner wall of the gut primordia and prevents proper transepithelial migration to the gonads. Conversely, RNAi knockdowns of Tao-1 cause disordered migration of PGCs out of the gut epithelium, their dispersal within the embryo and cell death. The results reveal a novel function of Tao-1 in cell migration, which is based on antagonistic activities of two proteins encoded by a single gene.

Indexed as

Cell MovementActin CytoskeletonAnimalsCell Surface ExtensionsDrosophilaGerm CellsMAP Kinase Kinase KinasesProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryMAP Kinase Kinase KinasesProtein Serine-Threonine KinasesTAO1 protein kinasecytoskeletal architectureectopic pole cell inductiongermline cell migrationSte20 kinase

Identifiers

PMID25589578
PMCPMC4313371

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.