Evidence map›Paper›PMID 30414309›Full record

ReviewCytoskeleton (Hoboken, N.J.)2018

Regulating a key mitotic regulator, polo-like kinase 1 (PLK1).

Erica G Colicino, Heidi Hehnly

Open access · hybridAbstract readReview
In one paragraph

Review in Cytoskeleton (Hoboken, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

73 citing papers in PubMed, 114 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Time-Lapse Imaging to Analyze Cell Fate in Response to Antimitotics.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. PLK1 inhibition impairs erythroid differentiation.Frontiers in cell and developmental biology · 2024
    Article

13 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Erica G ColicinoDepartment of Cell and Developmental Biology, Upstate Medical University, Syracuse, New York.ORCID 0000-0002-3333-1370
Heidi HehnlyDepartment of Cell and Developmental Biology, Upstate Medical University, Syracuse, New York.
SUNY Upstate Medical University · US

Funding

The relationship between Rab11-endosomes and the centrosome during divisionR01GM127621 · NIGMS · SYRACUSE UNIVERSITY · PI HEHNLY, HEIDI · 2018 to 2022
$1.8M
Mother Centriole Appendages Regulate the AMIS Compartment and Cilogenesis.R00GM107355 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI HEHNLY, HEIDI · 2015 to 2017
$723k
NIGMS NIH HHS R00 GM107355NIGMS NIH HHS R01 GM127621
6 · The paper itself

Abstract

During cell division, duplicated genetic material is separated into two distinct daughter cells. This process is essential for initial tissue formation during development and to maintain tissue integrity throughout an organism's lifetime. To ensure the efficacy and efficiency of this process, the cell employs a variety of regulatory and signaling proteins that function as mitotic regulators and checkpoint proteins. One vital mitotic regulator is polo-like kinase 1 (PLK1), a highly conserved member of the polo-like kinase family. Unique from its paralogues, it functions specifically during mitosis as a regulator of cell division. PLK1 is spatially and temporally enriched at three distinct subcellular locales; the mitotic centrosomes, kinetochores, and the cytokinetic midbody. These localization patterns allow PLK1 to phosphorylate specific downstream targets to regulate mitosis. In this review, we will explore how polo-like kinases were originally discovered and diverged into the five paralogues (PLK1-5) in mammals. We will then focus specifically on the most conserved, PLK1, where we will discuss what is known about how its activity is modulated, its role during the cell cycle, and new, innovative tools that have been developed to examine its function and interactions in cells.

Indexed as

AnimalsCell Cycle ProteinsCentrosomeCytokinesisHumansKinetochoresMitosisPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSignal TransductionCell Cycle ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene Proteinsbiosensorcell divisioncentrosomechemical geneticsFRETkinetochoremidbodymitosispolo-like kinase 1scaffolds

Identifiers

PMID30414309
PMCPMC7113694
OpenAlexW2899882096

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.