Evidence map›Paper›PMID 31338967›Full record

ArticleEMBO reports2019

FAM83D directs protein kinase CK1α to the mitotic spindle for proper spindle positioning.

Luke J Fulcher, Zhengcheng He, Lin Mei, Thomas J Macartney, Nicola T Wood, Alan R Prescott, Arlene J Whigham, Joby Varghese, Robert Gourlay, Graeme Ball and 4 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 59 citations in OpenAlex.

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  13. Review
  14. Casein kinase 1α mediates eryptosis: a review.Apoptosis : an international journal on programmed cell death · 2023
    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

14 authors at 2 institutions in 2 countries.

Luke J FulcherMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Zhengcheng HeMichael Cuccione Childhood Cancer Research Program, British Columbia Children's Hospital, University of British Columbia, Vancouver, BC, Canada.ORCID 0000-0002-8338-6185
Lin MeiMichael Cuccione Childhood Cancer Research Program, British Columbia Children's Hospital, University of British Columbia, Vancouver, BC, Canada.
Thomas J MacartneyMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Nicola T WoodMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Alan R PrescottDundee Imaging Facility, School of Life Sciences, University of Dundee, Dundee, UK.
Arlene J WhighamFlow Cytometry and Sorting Facility, School of Life Sciences, University of Dundee, Dundee, UK.
Joby VargheseMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Robert GourlayMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Graeme BallDundee Imaging Facility, School of Life Sciences, University of Dundee, Dundee, UK.
Rosemary ClarkeFlow Cytometry and Sorting Facility, School of Life Sciences, University of Dundee, Dundee, UK.
David G CampbellMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Christopher A MaxwellMichael Cuccione Childhood Cancer Research Program, British Columbia Children's Hospital, University of British Columbia, Vancouver, BC, Canada.
Gopal P SapkotaMedical Research Council, Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID 0000-0001-9931-3338
University of Dundee · GBUniversity of British Columbia · CA

Funding

Gouvernement du Canada|Canadian Institutes of Health Research CIHR OBC_134038Medical Research Council MC_UU_00018/6Medical Research Council MC_UU_12016/3Medical Research Council MR/K015869/1UK Research and Innovation|Medical Research Council (MRC) MC_UU_12016/3UK Research and Innovation|Medical Research Council (MRC) MR/K015869/1
6 · The paper itself

Abstract

The concerted action of many protein kinases helps orchestrate the error-free progression through mitosis of mammalian cells. The roles and regulation of some prominent mitotic kinases, such as cyclin-dependent kinases, are well established. However, these and other known mitotic kinases alone cannot account for the extent of protein phosphorylation that has been reported during mammalian mitosis. Here we demonstrate that CK1α, of the casein kinase 1 family of protein kinases, localises to the spindle and is required for proper spindle positioning and timely cell division. CK1α is recruited to the spindle by FAM83D, and cells devoid of FAM83D, or those harbouring CK1α-binding-deficient FAM83D

Indexed as

AnimalsCasein Kinase ICell CycleCell Cycle ProteinsCell Line, TumorFlow CytometryHeLa CellsHumansMiceMice, KnockoutMicrotubule-Associated ProteinsMitosisSpindle ApparatusCasein Kinase ICell Cycle ProteinsFAM83D protein, humanMicrotubule-Associated ProteinsCK1FAM83Dkinasemitosisspindle positioning

Identifiers

PMID31338967
PMCPMC6726907
OpenAlexW2963557796

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.