Evidence map›Paper›PMID 34313341›Full record

ArticleThe EMBO journal2021

Phospho-regulated Bim1/EB1 interactions trigger Dam1c ring assembly at the budding yeast outer kinetochore.

Alexander Dudziak, Lena Engelhard, Cole Bourque, Björn Udo Klink, Pascaline Rombaut, Nikolay Kornakov, Karolin Jänen, Franz Herzog, Christos Gatsogiannis, Stefan Westermann

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-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

11 citing papers in PubMed, 20 citations in OpenAlex.

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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

10 authors at 4 institutions in 1 country.

Alexander DudziakDepartment of Molecular Genetics I, Center of Molecular Biotechnology, University of Duisburg-Essen, Essen, Germany.ORCID 0000-0001-5082-3468
Lena EngelhardDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Cole BourqueDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Björn Udo KlinkDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Pascaline RombautGene Center Munich, Ludwig Maximilian University Munich, Munich, Germany.
Nikolay KornakovDepartment of Molecular Genetics I, Center of Molecular Biotechnology, University of Duisburg-Essen, Essen, Germany.ORCID 0000-0002-7960-2324
Karolin JänenDepartment of Molecular Genetics I, Center of Molecular Biotechnology, University of Duisburg-Essen, Essen, Germany.
Franz HerzogGene Center Munich, Ludwig Maximilian University Munich, Munich, Germany.ORCID 0000-0001-8270-1449
Christos GatsogiannisDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Stefan WestermannDepartment of Molecular Genetics I, Center of Molecular Biotechnology, University of Duisburg-Essen, Essen, Germany.ORCID 0000-0001-6921-9113
University of Duisburg-Essen · DEUniversity of Münster · DELudwig-Maximilians-Universität München · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinetochores form the link between chromosomes and microtubules of the mitotic spindle. The heterodecameric Dam1 complex (Dam1c) is a major component of the Saccharomyces cerevisiae outer kinetochore, assembling into 3 MDa-sized microtubule-embracing rings, but how ring assembly is specifically initiated in vivo remains to be understood. Here, we describe a molecular pathway that provides local control of ring assembly during the establishment of sister kinetochore bi-orientation. We show that Dam1c and the general microtubule plus end-associated protein (+TIP) Bim1/EB1 form a stable complex depending on a conserved motif in the Duo1 subunit of Dam1c. EM analyses reveal that Bim1 crosslinks protrusion domains of adjacent Dam1c heterodecamers and promotes the formation of oligomers with defined curvature. Disruption of the Dam1c-Bim1 interaction impairs kinetochore localization of Dam1c in metaphase and delays mitosis. Phosphorylation promotes Dam1c-Bim1 binding by relieving an intramolecular inhibition of the Dam1 C-terminus. In addition, Bim1 recruits Bik1/CLIP-170 to Dam1c and induces formation of full rings even in the absence of microtubules. Our data help to explain how new kinetochore end-on attachments are formed during the process of attachment error correction.

Indexed as

Chromosome SegregationKinetochoresMicrotubule-Associated ProteinsMicrotubule ProteinsMitosisMultiprotein ComplexesPhosphorylationProtein BindingSaccharomycetalesSpindle ApparatusMicrotubule-Associated ProteinsMicrotubule ProteinsMultiprotein ComplexesBik1Bim1bi-orientationchromosome segregationDam1/DASH complex

Identifiers

PMID34313341
PMCPMC8441410
OpenAlexW3184025797

What Socratic holds

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LicenceCC BY
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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 Socratic graph.