Evidence map›Paper›PMID 18824692›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motion.

Ekaterina L Grishchuk, Artem K Efremov, Vladimir A Volkov, Ilia S Spiridonov, Nikita Gudimchuk, Stefan Westermann, David Drubin, Georjana Barnes, J Richard McIntosh, Fazly I Ataullakhanov

Erratum issuedOpen access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

62 citing papers in PubMed, 92 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Review
  3. Review
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  5. Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Ultrafast Force-Clamp Spectroscopy of Microtubule-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

10 authors at 7 institutions in 3 countries.

Ekaterina L GrishchukMolecular, Cellular, and Developmental Biology Department, University of Colorado, Boulder, CO 80309, USA. katya@colorado.edu
Artem K Efremov
Vladimir A Volkov
Ilia S Spiridonov
Nikita Gudimchuk
Stefan Westermann
David Drubin
Georjana Barnes
J Richard McIntosh
Fazly I Ataullakhanov
Federal State Institution Hematology Research Center · RUResearch Institute of General Pathology and Pathophysiology, the Russian Academy of Medical Sciences · RUUniversity of California, Berkeley · USCenter for Theoretical Problems of Physicochemical Pharmacology · RULomonosov Moscow State University · RUResearch Institute of Molecular Pathology · ATUniversity of Colorado Boulder · US

Funding

MICROTUBULE POLYMERIZATION AND DYNAMICS IN VIVOR01GM033787 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI MCINTOSH, JOHN RICHARD · 1985 to 2017
$6.5M
NIGMS NIH HHS GM033787NIGMS NIH HHS R01 GM033787
6 · The paper itself

Abstract

Accurate chromosome segregation during mitotic division of budding yeast depends on the multiprotein kinetochore complex, Dam1 (also known as DASH). Purified Dam1 heterodecamers encircle microtubules (MTs) to form rings that can function as "couplers," molecular devices that transduce energy from MT disassembly into the motion of a cargo. Here we show that MT depolymerization develops a force against a Dam1 ring that is sixfold larger than the force exerted on a coupler that binds only one side of an MT. Wild-type rings slow depolymerization fourfold, but rings that include a mutant Dam1p with truncated C terminus slow depolymerization less, consistent with the idea that this tail is part of a strong bond between rings and MTs. A molecular-mechanical model for Dam1-MT interaction predicts that binding between this flexible tail and the MT wall should cause a Dam1 ring to wobble, and Fourier analysis of moving, ring-attached beads corroborates this prediction. Comparison of the forces generated against wild-type and mutant complexes confirms the importance of tight Dam1-MT association for processive cargo movement under load.

Indexed as

Biomechanical PhenomenaChromosome SegregationChromosomes, FungalKinetochoresMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalSaccharomycetalesMicrotubule-Associated Proteins

Identifiers

PMID18824692
PMCPMC2563122
OpenAlexW2118777837

What OpenQuestion holds

Textmetadata
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.