Evidence map›Paper›PMID 25808492›Full record

ArticleMolecular biology of the cell2015

Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity.

Anatoly V Zaytsev, Jeanne E Mick, Evgeny Maslennikov, Boris Nikashin, Jennifer G DeLuca, Ekaterina L Grishchuk

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 114 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
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10 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

Anatoly V ZaytsevPhysiology Department, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104.
Jeanne E MickDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.
Evgeny MaslennikovCenter for Theoretical Problems of Physico-Chemical Pharmacology, Russian Academy of Sciences, Moscow 119991, Russia.
Boris NikashinPhysiology Department, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104.
Jennifer G DeLucaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523 jdeluca@colostate.edu gekate@mail.med.upenn.edu.
Ekaterina L GrishchukPhysiology Department, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104 jdeluca@colostate.edu gekate@mail.med.upenn.edu.
University of Pennsylvania · USColorado State University · USCenter for Theoretical Problems of Physicochemical Pharmacology · RU

Funding

Coupling kinetochore microtubule dynamics to chromosome motionR01GM098389 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GRISHCHUK, EKATERINA L · 2012 to 2020
$3.1M
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 R01-GM088371NIGMS NIH HHS R01 GM098389NIGMS NIH HHS R01-GM098389
6 · The paper itself

Abstract

Microtubule (MT) attachment to kinetochores is vitally important for cell division, but how these interactions are controlled by phosphorylation is not well known. We used quantitative approaches in vitro combined with molecular dynamics simulations to examine phosphoregulation of the NDC80 complex, a core kinetochore component. We show that the outputs from multiple phosphorylation events on the unstructured tail of its Hec1 subunit are additively integrated to elicit gradual tuning of NDC80-MT binding both in vitro and in silico. Conformational plasticity of the Hec1 tail enables it to serve as a phosphorylation-controlled rheostat, providing a new paradigm for regulating the affinity of MT binders. We also show that cooperativity of NDC80 interactions is weak and is unaffected by NDC80 phosphorylation. This in vitro finding strongly supports our model that independent molecular binding events to MTs by individual NDC80 complexes, rather than their structured oligomers, regulate the dynamics and stability of kinetochore-MT attachments in dividing cells.

Indexed as

Cell Nucleus DivisionCytoskeletal ProteinsHumansKinetochoresMicrotubulesNuclear ProteinsPhosphorylationProtein BindingCytoskeletal ProteinsNDC80 protein, humanNuclear Proteins

Identifiers

PMID25808492
PMCPMC4436829
OpenAlexW2135232405

What OpenQuestion holds

Textmetadata
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.