Evidence map›Paper›PMID 32401635›Full record

ArticleMolecular biology of the cell2020

The Hec1/Ndc80 tail domain is required for force generation at kinetochores, but is dispensable for kinetochore-microtubule attachment formation and Ska complex recruitment.

Robert T Wimbish, Keith F DeLuca, Jeanne E Mick, Jack Himes, Ignacio Jiménez-Sánchez, A Arockia Jeyaprakash, Jennifer G DeLuca

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

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  13. Aurora B kinase: a potential drug target for cancer therapy.Journal of cancer research and clinical oncology · 2021
    Review
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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

7 authors at 2 institutions in 2 countries.

Robert T WimbishDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.
Keith F DeLucaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.
Jeanne E MickDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.
Jack HimesDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.
Ignacio Jiménez-SánchezWellcome Trust Centre for Cell Biology, University of Edinburgh, EH9 3BF Edinburgh, UK.
A Arockia JeyaprakashWellcome Trust Centre for Cell Biology, University of Edinburgh, EH9 3BF Edinburgh, UK.
Jennifer G DeLucaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.
Colorado State University · USUniversity of Edinburgh · GB

Funding

Mechanisms of Kinetochore-Microtubule Attachment and RegulationR35GM130365 · NIGMS · COLORADO STATE UNIVERSITY · PI Jennifer G DeLuca · 2019 to 2026
$3.8M
Kinetochore Function in Vertebrate CellsR01GM088371 · NIGMS · COLORADO STATE UNIVERSITY · PI DELUCA, JENNIFER G · 2010 to 2018
$3.1M
NIGMS NIH HHS R01 GM088371NIGMS NIH HHS R35 GM130365
6 · The paper itself

Abstract

The conserved kinetochore-associated NDC80 complex (composed of Hec1/Ndc80, Nuf2, Spc24, and Spc25) has well-documented roles in mitosis including 1) connecting mitotic chromosomes to spindle microtubules to establish force-transducing kinetochore-microtubule attachments and 2) regulating the binding strength between kinetochores and microtubules such that correct attachments are stabilized and erroneous attachments are released. Although the NDC80 complex plays a central role in forming and regulating attachments to microtubules, additional factors support these processes as well, including the spindle and kinetochore-associated (Ska) complex. Multiple lines of evidence suggest that Ska complexes strengthen attachments by increasing the ability of NDC80 complexes to bind microtubules, especially to depolymerizing microtubule plus ends, but how this is accomplished remains unclear. Using cell-based and in vitro assays, we demonstrate that the Hec1 tail domain is dispensable for Ska complex recruitment to kinetochores and for generation of kinetochore-microtubule attachments in human cells. We further demonstrate that Hec1 tail phosphorylation regulates kinetochore-microtubule attachment stability independently of the Ska complex. Finally, we map the location of the Ska complex in cells to a region near the coiled-coil domain of the NDC80 complex and demonstrate that this region is required for Ska complex recruitment to the NDC80 complex--microtubule interface.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosome SegregationCytoskeletal ProteinsHeLa CellsHumansKinetochoresMicrotubule-Associated ProteinsMicrotubulesMitosisNuclear ProteinsPhosphorylationCell Cycle ProteinsChromosomal Proteins, Non-HistoneCytoskeletal ProteinsMicrotubule-Associated ProteinsNDC80 protein, humanNuclear ProteinsSKA1 protein, human

Identifiers

PMID32401635
PMCPMC7359571
OpenAlexW3026332246

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.