Evidence map›Paper›PMID 23479640›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Binding of Drosophila Polo kinase to its regulator Matrimony is noncanonical and involves two separate functional domains.

Amanda M Bonner, Stacie E Hughes, Jennifer A Chisholm, S Kendall Smith, Brian D Slaughter, Jay R Unruh, Kimberly A Collins, Jennifer M Friederichs, Laurence Florens, Selene K Swanson and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Regulation of oocyte maturation: Role of conserved ERK signaling.Molecular reproduction and development · 2022
    Review
  5. Article
  6. Review
  7. Exo1 recruits Cdc5 polo kinase to MutLγ to ensure efficient meiotic crossover formation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Meiosis I Kinase Regulators: Conserved Orchestrators of Reductional Chromosome Segregation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Autoinhibition and relief mechanism for Polo-like kinase 4.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Article
  20. Polo-like kinases: structural variations lead to multiple functions.Nature reviews. Molecular cell biology · 2014
    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

15 authors at 3 institutions in 1 country.

Amanda M BonnerStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Stacie E Hughes
Jennifer A Chisholm
S Kendall Smith
Brian D Slaughter
Jay R Unruh
Kimberly A Collins
Jennifer M Friederichs
Laurence Florens
Selene K Swanson
Marissa C Pelot
Danny E Miller
Michael P Washburn
Sue L Jaspersen
R Scott Hawley
Stowers Institute for Medical Research · USUniversity of Kansas · USUniversity Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drosophila melanogaster Polo kinase physically interacts with, and is repressed by, the Matrimony (Mtrm) protein during oogenesis. Females heterozygous for a deletion of the mtrm gene display defects in chromosome segregation at meiosis I. However, a complete absence of Mtrm results in both meiotic catastrophe and female sterility. We show that three phosphorylated residues in an N-terminal region in Mtrm are required for Mtrm::Polo binding. However, this binding is noncanonical; it does not require either a complete S-pS/pT-P motif in Mtrm or key residues in the Polo-box domain of Polo that allow Polo to bind phosphorylated substrates. By using fluorescence cross-correlation spectroscopy to characterize the Mtrm::Polo interaction in vivo, we show that a sterile α-motif (SAM) domain located at the C terminus of Mtrm increases the stability of Mtrm::Polo binding. Although Mtrm's C-terminal SAM domain is not required to rescue the chromosome segregation defects observed in mtrm/+ females, it is essential to prevent both meiotic catastrophe and the female sterility observed in mtrm/mtrm females. We propose that Polo's interaction with the cluster of phosphorylated residues alone is sufficient to rescue the meiosis I defect. However, the strengthening of Mtrm::Polo binding mediated by the SAM domain is necessary to prevent meiotic catastrophe and ensure female fertility. Characterization of the Mtrm::Polo interaction, as well as that of other Polo regulators, may assist in the design of a new class of Polo inhibitors to be used as targeted anticancer therapeutic agents.

Indexed as

AnimalsCell Cycle ProteinsDrosophila melanogasterDrosophila ProteinsFemaleMaleMeiosisPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiarySpectrometry, FluorescenceCell Cycle ProteinsDrosophila Proteinsmtrm protein, Drosophilapolo protein, DrosophilaProtein Serine-Threonine Kinases

Identifiers

PMID23479640
PMCPMC3612667
OpenAlexW1967241208

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.