Evidence map›Paper›PMID 26175154›Full record

ArticleThe Journal of biological chemistry2015

The Inner Centromere Protein (INCENP) Coil Is a Single α-Helix (SAH) Domain That Binds Directly to Microtubules and Is Important for Chromosome Passenger Complex (CPC) Localization and Function in Mitosis.

Kumiko Samejima, Melpomeni Platani, Marcin Wolny, Hiromi Ogawa, Giulia Vargiu, Peter J Knight, Michelle Peckham, William C Earnshaw

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 77 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
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  7. Cahn-Hilliard dynamical models for condensed biomolecular systems.bioRxiv : the preprint server for biology · 2025
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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 at 2 institutions in 1 country.

Kumiko SamejimaFrom The Wellcome Trust Centre for Cell Biology, University of Edinburgh, King's Buildings, Max Born Crescent, Edinburgh EH9 3BF, Scotland, United Kingdom and kumiko.samejima@ed.ac.uk.
Melpomeni PlataniFrom The Wellcome Trust Centre for Cell Biology, University of Edinburgh, King's Buildings, Max Born Crescent, Edinburgh EH9 3BF, Scotland, United Kingdom and.
Marcin WolnyThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Hiromi OgawaFrom The Wellcome Trust Centre for Cell Biology, University of Edinburgh, King's Buildings, Max Born Crescent, Edinburgh EH9 3BF, Scotland, United Kingdom and.
Giulia VargiuFrom The Wellcome Trust Centre for Cell Biology, University of Edinburgh, King's Buildings, Max Born Crescent, Edinburgh EH9 3BF, Scotland, United Kingdom and.
Peter J KnightThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Michelle PeckhamThe Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom M.Peckham@leeds.ac.uk.
William C EarnshawFrom The Wellcome Trust Centre for Cell Biology, University of Edinburgh, King's Buildings, Max Born Crescent, Edinburgh EH9 3BF, Scotland, United Kingdom and bill.earnshaw@ed.ac.uk.
University of Edinburgh · GBUniversity of Leeds · GB

Funding

Wellcome Trust 073915Wellcome Trust 077707Wellcome Trust 092076
6 · The paper itself

Abstract

The chromosome passenger complex (CPC) is a master regulator of mitosis. Inner centromere protein (INCENP) acts as a scaffold regulating CPC localization and activity. During early mitosis, the N-terminal region of INCENP forms a three-helix bundle with Survivin and Borealin, directing the CPC to the inner centromere where it plays essential roles in chromosome alignment and the spindle assembly checkpoint. The C-terminal IN box region of INCENP is responsible for binding and activating Aurora B kinase. The central region of INCENP has been proposed to comprise a coiled coil domain acting as a spacer between the N- and C-terminal domains that is involved in microtubule binding and regulation of the spindle checkpoint. Here we show that the central region (213 residues) of chicken INCENP is not a coiled coil but a ∼ 32-nm-long single α-helix (SAH) domain. The N-terminal half of this domain directly binds to microtubules in vitro. By analogy with previous studies of myosin 10, our data suggest that the INCENP SAH might stretch up to ∼ 80 nm under physiological forces. Thus, the INCENP SAH could act as a flexible "dog leash," allowing Aurora B to phosphorylate dynamic substrates localized in the outer kinetochore while at the same time being stably anchored to the heterochromatin of the inner centromere. Furthermore, by achieving this flexibility via an SAH domain, the CPC avoids a need for dimerization (required for coiled coil formation), which would greatly complicate regulation of the proximity-induced trans-phosphorylation that is critical for Aurora B activation.

Indexed as

MitosisAmino Acid SequenceAnimalsAurora Kinase BCell LineCell ProliferationChickensChromosomal Proteins, Non-HistoneChromosomesMicrotubulesModels, BiologicalMolecular Sequence DataMutant ProteinsMutationPhosphorylationProtein BindingAurora Kinase BChromosomal Proteins, Non-HistoneMutant Proteinscentromerechromosome passenger complexcoiled coilCPCINCENPmicrotubulemitosismutantprotein structuresingle α-helix

Identifiers

PMID26175154
PMCPMC4571873
OpenAlexW1916209382

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.