Evidence map›Paper›PMID 26911623›Full record

ArticleOpen biology2016

Network of protein interactions within the Drosophila inner kinetochore.

Magdalena M Richter, Jaroslaw Poznanski, Anna Zdziarska, Mariusz Czarnocki-Cieciura, Zoltan Lipinszki, Michal Dadlez, David M Glover, Marcin R Przewloka

Abstract read
In one paragraph

Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Retention of a singlebioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Kinetochore Architecture Employs Diverse Linker Strategies Across Evolution.Frontiers in cell and developmental biology · 2022
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Phosphorylation of CENP-C by Aurora B facilitates kinetochore attachment error correction in mitosis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. 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

8 authors.

Magdalena M RichterDepartment of Genetics, University of Cambridge, Cambridge, UK Institute of Biochemistry and Biophysics, Polish Academy of Science, Warsaw, Poland.
Jaroslaw PoznanskiInstitute of Biochemistry and Biophysics, Polish Academy of Science, Warsaw, Poland.
Anna ZdziarskaInstitute of Biochemistry and Biophysics, Polish Academy of Science, Warsaw, Poland.
Mariusz Czarnocki-CieciuraInstitute of Biochemistry and Biophysics, Polish Academy of Science, Warsaw, Poland Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Zoltan LipinszkiDepartment of Genetics, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-2067-0832
Michal DadlezInstitute of Biochemistry and Biophysics, Polish Academy of Science, Warsaw, Poland Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
David M GloverDepartment of Genetics, University of Cambridge, Cambridge, UK.
Marcin R PrzewlokaDepartment of Genetics, University of Cambridge, Cambridge, UK mrp50@cam.ac.uk.ORCID http://orcid.org/0000-0002-0329-9162

Funding

Cancer Research UK 11431Cancer Research UK 18795Medical Research Council G1001696
6 · The paper itself

Abstract

The kinetochore provides a physical connection between microtubules and the centromeric regions of chromosomes that is critical for their equitable segregation. The trimeric Mis12 sub-complex of the Drosophila kinetochore binds to the mitotic centromere using CENP-C as a platform. However, knowledge of the precise connections between Mis12 complex components and CENP-C has remained elusive despite the fundamental importance of this part of the cell division machinery. Here, we employ hydrogen-deuterium exchange coupled with mass spectrometry to reveal that Mis12 and Nnf1 form a dimer maintained by interacting coiled-coil (CC) domains within the carboxy-terminal parts of both proteins. Adjacent to these interacting CCs is a carboxy-terminal domain that also interacts with Nsl1. The amino-terminal parts of Mis12 and Nnf1 form a CENP-C-binding surface, which docks the complex and thus the entire kinetochore to mitotic centromeres. Mutational analysis confirms these precise interactions are critical for both structure and function of the complex. Thus, we conclude the organization of the Mis12-Nnf1 dimer confers upon the Mis12 complex a bipolar, elongated structure that is critical for kinetochore function.

Indexed as

Protein Interaction MapsAmino Acid SequenceAnimalsCentromereChromosomal Proteins, Non-HistoneDrosophilaDrosophila ProteinsKinetochoresMicrotubulesModels, MolecularMolecular Sequence DataNuclear ProteinsProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein Interaction Mappingcentromere protein CChromosomal Proteins, Non-HistoneDrosophila ProteinsNSL1 protein, DrosophilaNuclear ProteinsTranscription FactorsVesicular Transport ProteinscentromerechromosomeHDX-MSkinetochoremitosisstructure

Identifiers

PMID26911623
PMCPMC4772809

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Registered trials

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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.