Evidence map›Paper›PMID 24928906›Full record

ArticleJournal of cell science2014

Rassf5 and Ndr kinases regulate neuronal polarity through Par3 phosphorylation in a novel pathway.

Rui Yang, Eryan Kong, Jing Jin, Alexander Hergovich, Andreas W Püschel

Abstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

22 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. ALS-linked C9orf72-SMCR8 complex is a negative regulator of primary ciliogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. The Roles of Par3, Par6, and aPKC Polarity Proteins in Normal Neurodevelopment and in Neurodegenerative and Neuropsychiatric Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Review
  10. Article
  11. PTEN-GSK3β-MOB1 axis controls neurite outgrowth in vitro and in vivo.Cellular and molecular life sciences : CMLS · 2018
    Article
  12. Article
  13. PAR3-PAR6-atypical PKC polarity complex proteins in neuronal polarization.Cellular and molecular life sciences : CMLS · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Novel DLK-independent neuronal regeneration in Caenorhabditis elegans shares links with activity-dependent ectopic outgrowth.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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.

Rui YangInstitut für Molekulare Zellbiologie, Westfälische Wilhelms-Universität Münster, Schloßplatz 5, D-48149 Münster, Germany.
Eryan KongInstitut für Molekulare Zellbiologie, Westfälische Wilhelms-Universität Münster, Schloßplatz 5, D-48149 Münster, Germany.
Jing JinInstitut für Molekulare Zellbiologie, Westfälische Wilhelms-Universität Münster, Schloßplatz 5, D-48149 Münster, Germany.
Alexander HergovichUCL Cancer Institute, University College London, London WC1E 6BT, UK.
Andreas W PüschelInstitut für Molekulare Zellbiologie, Westfälische Wilhelms-Universität Münster, Schloßplatz 5, D-48149 Münster, Germany Cells-in-Motion Cluster of Excellence, University of Münster, D-48149 Münster, Germany apuschel@uni-muenster.de.
University of Münster · DEUniversity College London · GB

Funding

Wellcome TrustWellcome Trust 090090/Z/09/Z
6 · The paper itself

Abstract

The morphology and polarized growth of cells depend on pathways that control the asymmetric distribution of regulatory factors. The evolutionarily conserved Ndr kinases play important roles in cell polarity and morphogenesis in yeast and invertebrates but it is unclear whether they perform a similar function in mammalian cells. Here, we analyze the function of mammalian Ndr1 and Ndr2 (also known as STK38 or STK38L, respectively) in the establishment of polarity in neurons. We show that they act downstream of the tumor suppressor Rassf5 and upstream of the polarity protein Par3 (also known as PARD3). Rassf5 and Ndr1 or Ndr2 are required during the polarization of hippocampal neurons to prevent the formation of supernumerary axons. Mechanistically, the Ndr kinases act by phosphorylating Par3 at Ser383 to inhibit its interaction with dynein, thereby polarizing the distribution of Par3 and reinforcing axon specification. Our results identify a novel Rassf5-Ndr-Par3 signaling cascade that regulates the transport of Par3 during the establishment of neuronal polarity. Their role in neuronal polarity suggests that Ndr kinases perform a conserved function as regulators of cell polarity.

Indexed as

Cell PolarityAdaptor Proteins, Signal TransducingAnimalsApoptosis Regulatory ProteinsCell Adhesion MoleculesCell Cycle ProteinsMiceMice, KnockoutNeuronsPhosphorylationProtein BindingProtein Serine-Threonine KinasesSignal TransductionAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCell Adhesion MoleculesCell Cycle ProteinsNDR1 protein kinase, mouseNDR2 protein kinase, mousePard3 protein, mouseProtein Serine-Threonine KinasesRassf5 protein, mouseAxon formationCell polarityNdr kinasesPar

Identifiers

PMID24928906
PMCPMC4132390
OpenAlexW2071198165

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.