Evidence map›Paper›PMID 24066227›Full record

ArticleeLife2013

Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling.

Ivana Primorac, John R Weir, Elena Chiroli, Fridolin Gross, Ingrid Hoffmann, Suzan van Gerwen, Andrea Ciliberto, Andrea Musacchio

Abstract read
In one paragraph

Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.

0numbers the graph read from it
0cells of the map it votes in
143citing 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

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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

143 citing papers in PubMed.

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83 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Ivana PrimoracDepartment of Mechanistic Cell Biology , Max Planck Institute of Molecular Physiology , Dortmund , Germany.
John R Weir
Elena Chiroli
Fridolin Gross
Ingrid Hoffmann
Suzan van Gerwen
Andrea Ciliberto
Andrea Musacchio

Funding

European Research Council 233316
6 · The paper itself

Abstract

Regulation of macromolecular interactions by phosphorylation is crucial in signaling networks. In the spindle assembly checkpoint (SAC), which enables errorless chromosome segregation, phosphorylation promotes recruitment of SAC proteins to tensionless kinetochores. The SAC kinase Mps1 phosphorylates multiple Met-Glu-Leu-Thr (MELT) motifs on the kinetochore subunit Spc105/Knl1. The phosphorylated MELT motifs (MELT(P)) then promote recruitment of downstream signaling components. How MELT(P) motifs are recognized is unclear. In this study, we report that Bub3, a 7-bladed β-propeller, is the MELT(P) reader. It contains an exceptionally well-conserved interface that docks the MELT(P) sequence on the side of the β-propeller in a previously unknown binding mode. Mutations targeting the Bub3 interface prevent kinetochore recruitment of the SAC kinase Bub1. Crucially, they also cause a checkpoint defect, showing that recognition of phosphorylated targets by Bub3 is required for checkpoint signaling. Our data provide the first detailed mechanistic insight into how phosphorylation promotes recruitment of checkpoint proteins to kinetochores. DOI:http://dx.doi.org/10.7554/eLife.01030.001.

Indexed as

Signal TransductionSpindle ApparatusAmino Acid SequenceCell Cycle ProteinsHumansMolecular Sequence DataMutationOligopeptidesPhosphorylationPoly-ADP-Ribose Binding ProteinsProtein ConformationSequence Homology, Amino AcidBUB3 protein, humanCell Cycle ProteinsOligopeptidesPoly-ADP-Ribose Binding ProteinsBub1Bub3kinetochoreKnl1Mad3S. cerevisiaespindle assembly checkpoint

Identifiers

PMID24066227
PMCPMC3779320

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Read underepoch 390

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.