Evidence map›Paper›PMID 16968737›Full record

ArticleJournal of cell science2006

Trimerisation is important for the function of clathrin at the mitotic spindle.

Stephen J Royle, Leon Lagnado

Abstract read
In one paragraph

Article in Journal of cell science, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

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  6. The Clathrin-dependent Spindle Proteome.Molecular & cellular proteomics : MCP · 2016
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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

2 authors at 1 institution in 1 country.

Stephen J RoyleMRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK. S.J.Royle@liverpool.ac.uk
Leon Lagnado
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178794Medical Research Council U.1051.02.006(78794)
6 · The paper itself

Abstract

Clathrin is a triskelion consisting of three heavy chains each with an associated light chain. During mitosis, clathrin contributes to kinetochore fibre stability. As the N-terminal domain at the foot of each leg can bind to the mitotic spindle, we proposed previously a ;bridge hypothesis' wherein clathrin acts as a brace between two or three microtubules within a kinetochore fibre to increase fibre stability. Here, we have tested this hypothesis by replacing endogenous clathrin heavy chain in human cells with a panel of clathrin constructs. Mutants designed to abolish trimerisation were unable to rescue the mitotic defects caused by depletion of endogenous clathrin. By contrast, stunted triskelia with contracted legs could partially rescue normal mitosis. These results indicate that the key structural features of clathrin that are necessary for its function in mitosis are a trimeric molecule with a spindle interaction domain at each end, supporting the bridge hypothesis for clathrin function in mitosis.

Indexed as

Cells, CulturedClathrinClathrin Heavy ChainsClathrin Light ChainsEndocytosisHumansMitosisModels, MolecularPolymersProtein BindingProtein ConformationProtein FoldingRNA InterferenceRNA, Small InterferingSpindle ApparatusClathrinClathrin Heavy ChainsClathrin Light ChainsPolymersRNA, Small Interfering

Identifiers

PMID16968737
PMCPMC3475310
OpenAlexW2113348004

What OpenQuestion holds

Textmetadata
LicenceTDM
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.