Evidence map›Paper›PMID 28931593›Full record

ArticleMolecular biology of the cell2017

Active Ran regulates anillin function during cytokinesis.

Daniel Beaudet, Tara Akhshi, Julia Phillipp, Christopher Law, Alisa Piekny

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Ran GTPase and Its Importance in Cellular Signaling and Malignant Phenotype.International journal of molecular sciences · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Cortical excitability and cell division.Current biology : CB · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. The Unusual Suspects in Cytokinesis: Fitting the Pieces Together.Frontiers in cell and developmental biology · 2020
    Review
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 3 institutions in 1 country.

Daniel BeaudetDepartment of Biology, Concordia University, Montreal, QC H4B 1R6, Canada.
Tara AkhshiProgram in Cell Biology, the Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.
Julia PhillippDepartment of Biology, Concordia University, Montreal, QC H4B 1R6, Canada.
Christopher LawCentre for Microscopy and Cellular Imaging, Concordia University, Montreal, QC H4B 1R6, Canada.
Alisa PieknyProgram in Cell Biology, the Hospital for Sick Children, Toronto, ON M5G 0A4, Canada alisa.piekny@concordia.ca.
Concordia University · CAHospital for Sick Children · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytokinesis cleaves a cell into two daughters at the end of mitosis, and must be spatially coordinated with chromosome segregation to prevent aneuploidy. The dogma is that the mitotic spindle governs the assembly and constriction of an actomyosin ring. Here, we reveal a function for active Ran in spatially restricting the ring. Our model is that during anaphase, "free" importins, whose gradient inversely correlates with active Ran and chromatin position, function as a molecular ruler for the recruitment and localization of anillin, a contractile protein and a crucial regulator of cytokinesis. We found that decreasing Ran-GTP levels or tethering active Ran to the equatorial membrane affects anillin's localization and causes cytokinesis phenotypes. Anillin contains a conserved nuclear localization signal (NLS) at its C-terminus that binds to importin-β and is required for cortical polarity and cytokinesis. Mutating the NLS decreases anillin's cortical affinity, causing it to be more dominantly regulated by microtubules. Anillin contains a RhoA-GTP binding domain, which autoinhibits the NLS and the neighboring microtubule-binding domain, and RhoA-GTP binding may relieve this inhibition during mitosis. Retention of the C-terminal NLS in anillin homologues suggests that this is a conserved mechanism for controlling anillin function.

Indexed as

Animalsbeta KaryopherinsCells, CulturedCytokinesisHeLa CellsHumansKaryopherinsMiceMicrofilament ProteinsMicrotubulesMitosisNuclear Localization Signalsran GTP-Binding ProteinrhoA GTP-Binding ProteinSpindle ApparatusANLN protein, humanbeta KaryopherinsKaryopherinsMicrofilament ProteinsNuclear Localization Signalsran GTP-Binding ProteinRAN protein, humanrhoA GTP-Binding Protein

Identifiers

PMID28931593
PMCPMC5683762
OpenAlexW2754518029

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.