Evidence map›Paper›PMID 34143863›Full record

ArticleThe Biochemical journal2021

Co-ordinated control of the Aurora B abscission checkpoint by PKCε complex assembly, midbody recruitment and retention.

Lisa Watson, Tanya N Soliman, Khalil Davis, Joanna Kelly, Nicola Lockwood, Xiaoping Yang, Steven Lynham, John D Scott, Victoria Crossland, Neil Q McDonald and 4 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
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 4 institutions in 2 countries.

Lisa WatsonProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
Tanya N SolimanProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
Khalil DavisProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
Joanna KellyProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
Nicola LockwoodProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
Xiaoping YangProteomics Facility, King's College London, Denmark Hill Campus, London SE5 9NU, U.K.
Steven LynhamProteomics Facility, King's College London, Denmark Hill Campus, London SE5 9NU, U.K.
John D ScottDepartment of Pharmacology, University of Washington, Seattle, WA 98195, U.S.A.ORCID 0000-0002-0367-8146
Victoria CrosslandProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
Neil Q McDonaldSignalling and Structural Biology Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.
David J MannDepartment of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, U.K.
Alan ArmstrongDepartment of Chemistry, Imperial College London White City Campus, London W12 0BZ, U.K.
Ulrike EggertRandall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, King's College London, London SE1 1UL, U.K.
Peter J ParkerProtein Phosphorylation Laboratory, Francis Crick Institute, Midland Road, London NE1 1AT, U.K.ORCID 0000-0001-5907-6980
The Francis Crick Institute · GBKing's College London · GBImperial College London · GBUniversity of Washington · US

Funding

AKAP Modulation of Renal SignalingR01DK119186 · NIDDK · UNIVERSITY OF WASHINGTON · PI SCOTT, JOHN D · 2019 to 2022
$1.5M
NIDDK NIH HHS R01 DK119186Wellcome Trust 110060/Z/15/Z
6 · The paper itself

Abstract

A requirement for PKCε in exiting from the Aurora B dependent abscission checkpoint is associated with events at the midbody, however, the recruitment, retention and action of PKCε in this compartment are poorly understood. Here, the prerequisite for 14-3-3 complex assembly in this pathway is directly linked to the phosphorylation of Aurora B S227 at the midbody. However, while essential for PKCε control of Aurora B, 14-3-3 association is shown to be unnecessary for the activity-dependent enrichment of PKCε at the midbody. This localisation is demonstrated to be an autonomous property of the inactive PKCε D532N mutant, consistent with activity-dependent dissociation. The C1A and C1B domains are necessary for this localisation, while the C2 domain and inter-C1 domain (IC1D) are necessary for retention at the midbody. Furthermore, it is shown that while the IC1D mutant retains 14-3-3 complex proficiency, it does not support Aurora B phosphorylation, nor rescues division failure observed with knockdown of endogenous PKCε. It is concluded that the concerted action of multiple independent events facilitates PKCε phosphorylation of Aurora B at the midbody to control exit from the abscission checkpoint.

Indexed as

Cytokinesis14-3-3 ProteinsAurora Kinase BHEK293 CellsHumansPhosphorylationProtein Kinase C-epsilonSignal TransductionSpindle Apparatus14-3-3 ProteinsAURKB protein, humanAurora Kinase BProtein Kinase C-epsilon14-3-3abscission checkpointaurora kinasesmidbodyprotein kinase C

Identifiers

PMID34143863
PMCPMC8238520
OpenAlexW3166013377

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.