Evidence map›Paper›PMID 22214762›Full record

ArticleCell cycle (Georgetown, Tex.)2012

A functional cooperativity between Aurora A kinase and LIM kinase1: implication in the mitotic process.

Lisa Ritchey, Richard Ottman, Michael Roumanos, Ratna Chakrabarti

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. The Aurora kinase inhibitors in cancer research and therapy.Journal of cancer research and clinical oncology · 2016
    Review
  11. Article
  12. Article
  13. Issues in interpreting the in vivo activity of Aurora-A.Expert opinion on therapeutic targets · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Aurora A kinase (AURKA) in normal and pathological cell division.Cellular and molecular life sciences : CMLS · 2013
    Review
  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

4 authors at 2 institutions in 2 countries.

Lisa RitcheyBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, USA.
Richard Ottman
Michael Roumanos
Ratna Chakrabarti
Moscow State University of Technologies and Management named after K.G. Razumovskiy · RUUniversity of Central Florida · US

Funding

LIM kinase 1 and Cell Cycle RegulationR15CA125681 · NCI · UNIVERSITY OF CENTRAL FLORIDA · PI CHAKRABARTI, RATNA · 2008 to 2008
$213k
NCI NIH HHS R15 CA125681
6 · The paper itself

Abstract

Aurora kinase A (Aur-A), a mitotic kinase, regulates initiation of mitosis through centrosome separation and proper assembly of bipolar spindles. LIM kinase 1 (LIMK1), a modulator of actin and microtubule dynamics, is involved in the mitotic process through inactivating phosphorylation of cofilin. Phosphorylated LIMK1 is recruited to the centrosomes during early prophase, where it colocalizes with γ-tubulin. Here, we report a novel functional cooperativity between Aur-A and LIMK1 through mutual phosphorylation. LIMK1 is recruited to the centrosomes during early prophase and then to the spindle poles, where it colocalizes with Aur-A. Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization. Aur-A also acts as a substrate of LIMK1, and the function of LIMK1 is important for its specific localization and regulation of spindle morphology. Taken together, the novel molecular interaction between these two kinases and their regulatory roles on one another's function may provide new insight on the role of Aur-A in manipulation of actin and microtubular structures during spindle formation.

Indexed as

MitosisProtein Processing, Post-TranslationalAurora Kinase AAurora KinasesCell LineCentrosomeHumansLim KinasesMicroscopy, FluorescencePhosphorylationPhosphoserineProtein BindingProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesProtein TransportSpindle ApparatusAURKA protein, humanAurora Kinase AAurora KinasesLIMK1 protein, humanLim KinasesPhosphoserineProtein Serine-Threonine Kinases

Identifiers

PMID22214762
PMCPMC3293380
OpenAlexW2035704952

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.