Evidence map›Paper›PMID 25611342›Full record

ArticleeLife2015

A molecular basis for the differential roles of Bub1 and BubR1 in the spindle assembly checkpoint.

Katharina Overlack, Ivana Primorac, Mathijs Vleugel, Veronica Krenn, Stefano Maffini, Ingrid Hoffmann, Geert J P L Kops, Andrea Musacchio

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

95 citing papers in PubMed, 162 citations in OpenAlex.

  1. Review
  2. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  3. BUB1B is a novel prognostic-related biomarker and correlated with immune infiltrates in lung adenocarcinoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Article
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35 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

8 authors at 3 institutions in 2 countries.

Katharina OverlackDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Ivana PrimoracDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Mathijs VleugelMolecular Cancer Research, University Medical Center Utrecht, Utrecht, Netherlands.
Veronica KrennDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Stefano MaffiniDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Ingrid HoffmannDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Geert J P L KopsDepartment of Molecular Cancer Research, University Medical Center Utrecht, Utrecht, Netherlands.
Andrea MusacchioDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Max Planck Institute of Molecular Physiology · DEUniversity Medical Center Utrecht · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spindle assembly checkpoint (SAC) monitors and promotes kinetochore-microtubule attachment during mitosis. Bub1 and BubR1, SAC components, originated from duplication of an ancestor gene. Subsequent sub-functionalization established subordination: Bub1, recruited first to kinetochores, promotes successive BubR1 recruitment. Because both Bub1 and BubR1 hetero-dimerize with Bub3, a targeting adaptor for phosphorylated kinetochores, the molecular basis for such sub-functionalization is unclear. We demonstrate that Bub1, but not BubR1, enhances binding of Bub3 to phosphorylated kinetochores. Grafting a short motif of Bub1 onto BubR1 promotes Bub1-independent kinetochore recruitment of BubR1. This gain-of-function BubR1 mutant cannot sustain a functional checkpoint. We demonstrate that kinetochore localization of BubR1 relies on direct hetero-dimerization with Bub1 at a pseudo-symmetric interface. This pseudo-symmetric interaction underpins a template-copy relationship crucial for kinetochore-microtubule attachment and SAC signaling. Our results illustrate how gene duplication and sub-functionalization shape the workings of an essential molecular network.

Indexed as

Amino Acid MotifsAmino Acid SequenceCell Cycle ProteinsHeLa CellsHumansKinetochoresModels, BiologicalMolecular Sequence DataM Phase Cell Cycle CheckpointsMutant ProteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein Structure, SecondaryProtein TransportProtein-Tyrosine KinasesBUB1 protein, humanCell Cycle ProteinsMutant ProteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesTTK protein, humanbiochemistrycell biologycell cyclecell divisioncentromerehumankinetochorespindle assembly checkpoint

Identifiers

PMID25611342
PMCPMC4337726
OpenAlexW2155915788

What OpenQuestion holds

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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.