Evidence map›Paper›PMID 19204120›Full record

ArticleGenes & development2009

Protein phosphatase 4 mediates localization of the Miranda complex during Drosophila neuroblast asymmetric divisions.

Rita Sousa-Nunes, William Chia, W Greg Somers

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

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

43 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Asymmetry of centrosomes inMolecular biology of the cell · 2025
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  7. SMEK1 promotes lung adenocarcinoma proliferation and invasion by activating Wnt/β-catenin signaling pathway.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Principles and mechanisms of asymmetric cell division.Development (Cambridge, England) · 2020
    Review
  12. Article
  13. Review
  14. Genetics · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Smek1/2 is a nuclear chaperone and cofactor for cleaved Wnt receptor Ryk, regulating cortical neurogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Rita Sousa-NunesDepartment of Biological Sciences, Temasek Life Sciences Laboratory, National University of Singapore, Singapore.
William Chia
W Greg Somers
National University of Singapore · SGTemasek Life Sciences Laboratory · SG

Funding

Wellcome TrustWellcome Trust 070152
6 · The paper itself

Abstract

Asymmetric localization of cell fate determinants is a crucial step in neuroblast asymmetric divisions. Whereas several protein kinases have been shown to mediate this process, no protein phosphatase has so far been implicated. In a clonal screen of larval neuroblasts we identified the evolutionarily conserved Protein Phosphatase 4 (PP4) regulatory subunit PP4R3/Falafel (Flfl) as a key mediator specific for the localization of Miranda (Mira) and associated cell fate determinants during both interphase and mitosis. Flfl is predominantly nuclear during interphase/prophase and cytoplasmic after nuclear envelope breakdown. Analyses of nuclear excluded as well as membrane targeted versions of the protein suggest that the asymmetric cortical localization of Mira and its associated proteins during mitosis depends on cytoplasmic/membrane-associated Flfl, whereas nuclear Flfl is required to exclude the cell fate determinant Prospero (Pros), and consequently Mira, from the nucleus during interphase/prophase. Attenuating the function of either the catalytic subunit of PP4 (PP4C; Pp4-19C in Drosophila) or of another regulatory subunit, PP4R2 (PPP4R2r in Drosophila), leads to similar defects in the localization of Mira and associated proteins. Flfl is capable of directly interacting with Mira, and genetic analyses indicate that flfl acts in parallel to or downstream from the tumor suppressor lethal (2) giant larvae (lgl). Our findings suggest that Flfl may target PP4 to the MIra protein complex to facilitate dephosphorylation step(s) crucial for its cortical association/asymmetric localization.

Indexed as

AnimalsAnimals, Genetically ModifiedCell CycleCell Cycle ProteinsCell DivisionDrosophilaDrosophila ProteinsFemaleGenes, InsectMaleMultiprotein ComplexesMutationMyosin Heavy ChainsNerve Tissue ProteinsNeuronsNuclear ProteinsCell Cycle ProteinsDrosophila Proteinsl(2)gl protein, DrosophilaMira protein, DrosophilaMultiprotein ComplexesMyosin Heavy Chainsmyosin VINerve Tissue ProteinsNuclear ProteinsPhosphoprotein PhosphatasesPKC-3 proteinpros protein, DrosophilaProtein Kinase Cprotein phosphatase 4Protein SubunitsTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID19204120
PMCPMC2648543
OpenAlexW2119892402

What OpenQuestion holds

Textmetadata
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.