Evidence map›Paper›PMID 21256019›Full record

ArticleCurrent biology : CB2011

The Ndc80 loop region facilitates formation of kinetochore attachment to the dynamic microtubule plus end.

Jean-François Maure, Shinya Komoto, Yusuke Oku, Akihisa Mino, Sebastiano Pasqualato, Kayo Natsume, Lesley Clayton, Andrea Musacchio, Tomoyuki U Tanaka

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

69 citing papers in PubMed, 100 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Structure of the human outer kinetochore KMN network complex.Nature structural & molecular biology · 2024
    Article
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  8. Ccp1-Ndc80 switch at the N terminus of CENP-T regulates kinetochore assembly.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  13. Review
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9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 3 countries.

Jean-François MaureWellcome Trust Centre for Gene Regulation & Expression, University of Dundee, Dundee DD1 5EH, UK.
Shinya Komoto
Yusuke Oku
Akihisa Mino
Sebastiano Pasqualato
Kayo Natsume
Lesley Clayton
Andrea Musacchio
Tomoyuki U Tanaka
University of Dundee · GBEuropean Institute of Oncology · ITMax Planck Society · DE

Funding

Cancer Research UKMedical Research Council G0701147
6 · The paper itself

Abstract

Proper chromosome segregation in mitosis relies on correct kinetochore-microtubule (KT-MT) interactions. The KT initially interacts with the lateral surface of a single MT (lateral attachment) extending from a spindle pole and is subsequently anchored at the plus end of the MT (end-on attachment). The conversion from lateral to end-on attachment is crucial because end-on attachment is more robust and thought to be necessary to sustain KT-MT attachment when tension is applied across sister KTs upon their biorientation. The mechanism for this conversion is still elusive. The Ndc80 complex is an essential component of the KT-MT interface, and here we studied a role of the Ndc80 loop region, a distinct motif looping out from the coiled-coil shaft of the complex, in Saccharomyces cerevisiae. With deletions or mutations of the loop region, the lateral KT-MT attachment occurred normally; however, subsequent conversion to end-on attachment was defective, leading to failure in sister KT biorientation. The Ndc80 loop region was required for Ndc80-Dam1 interaction and KT loading of the Dam1 complex, which in turn supported KT tethering to the dynamic MT plus end. The Ndc80 loop region, therefore, has an important role in the conversion from lateral to end-on attachment, a crucial maturation step of KT-MT interaction.

Indexed as

Amino Acid SequenceKinetochoresMicrotubulesMolecular Sequence DataNuclear ProteinsProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentNDC80 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21256019
PMCPMC3052438
OpenAlexW2023954525

What OpenQuestion holds

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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.