Evidence map›Paper›PMID 33591274›Full record

ArticleeLife2021

Structural basis of Stu2 recruitment to yeast kinetochores.

Jacob A Zahm, Michael G Stewart, Joseph S Carrier, Stephen C Harrison, Matthew P Miller

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 21 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
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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

5 authors at 2 institutions in 1 country.

Jacob A Zahm *Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Howard Hughes Medical Institute, Boston, United States.ORCID 0000-0002-9600-5433
Michael G Stewart *Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.ORCID 0000-0001-6581-6332
Joseph S CarrierDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Stephen C HarrisonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Howard Hughes Medical Institute, Boston, United States.ORCID 0000-0001-7215-9393
Matthew P MillerDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.ORCID 0000-0003-2012-7546
University of Utah · USHoward Hughes Medical Institute · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
TRAINING PROGRAM IN GENETICST32GM007464 · NIGMS · UNIVERSITY OF UTAH · PI GRUNWALD, DAVID J., STANFIELD, GILLIAN · 1985 to 2020
$6.1M
University of Utah Genetics Training ProgramT32GM141848 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI GOLIC, KENT G, GRUNWALD, DAVID J. · 2021 to 2025
$2.9M
NIGMS NIH HHS P30 GM124165NIGMS NIH HHS T32 GM007464NIGMS NIH HHS T32 GM141848
6 · The paper itself

Abstract

Chromosome segregation during cell division requires engagement of kinetochores of sister chromatids with microtubules emanating from opposite poles. As the corresponding microtubules shorten, these 'bioriented' sister kinetochores experience tension-dependent stabilization of microtubule attachments. The yeast XMAP215 family member and microtubule polymerase, Stu2, associates with kinetochores and contributes to tension-dependent stabilization in vitro. We show here that a C-terminal segment of Stu2 binds the four-way junction of the Ndc80 complex (Ndc80c) and that residues conserved both in yeast Stu2 orthologs and in their metazoan counterparts make specific contacts with Ndc80 and Spc24. Mutations that perturb this interaction prevent association of Stu2 with kinetochores, impair cell viability, produce biorientation defects, and delay cell cycle progression. Ectopic tethering of the mutant Stu2 species to the Ndc80c junction restores wild-type function in vivo. These findings show that the role of Stu2 in tension-sensing depends on its association with kinetochores by binding with Ndc80c.

Indexed as

Chromosome SegregationKinetochoresMicrotubule-Associated ProteinsMutationNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMicrotubule-Associated ProteinsNDC80 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae ProteinsSTU2 protein, S cerevisiaecell biologykinetochoremolecular biophysicsNdc80 complexS. cerevisiaestructural biologystructureStu2tension

Identifiers

PMID33591274
PMCPMC7909949
OpenAlexW3130824878

What OpenQuestion holds

Textmetadata
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.