Evidence map›Paper›PMID 29510984›Full record

ArticleThe EMBO journal2018

Mitotic spindle association of TACC3 requires Aurora-A-dependent stabilization of a cryptic α-helix.

Selena G Burgess, Manjeet Mukherjee, Sarah Sabir, Nimesh Joseph, Cristina Gutiérrez-Caballero, Mark W Richards, Nicolas Huguenin-Dezot, Jason W Chin, Eileen J Kennedy, Mark Pfuhl and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.2field-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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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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

13 authors at 6 institutions in 2 countries.

Selena G BurgessAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Manjeet MukherjeeAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Sarah SabirAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Nimesh JosephCancer Research UK Cambridge Institute, Li Ka Shing Centre, University of Cambridge, Cambridge, UK.
Cristina Gutiérrez-CaballeroCentre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.
Mark W RichardsAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Nicolas Huguenin-DezotMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Jason W ChinMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Eileen J KennedyDepartment of Pharmaceutical and Biomedical Sciences, College of Pharmacy, University of Georgia, Athens, GA, USA.
Mark PfuhlCardiovascular & Randall Division, Kings College London, London, UK.ORCID 0000-0001-9592-6639
Stephen J RoyleCentre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.ORCID 0000-0001-8927-6967
Fanni GergelyCancer Research UK Cambridge Institute, Li Ka Shing Centre, University of Cambridge, Cambridge, UK.ORCID 0000-0002-2441-8095
Richard BaylissAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK r.w.bayliss@leeds.ac.uk.ORCID 0000-0003-0604-2773
University of Leeds · GBMRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GBUniversity of Warwick · GBKing's College London · GBUniversity of Georgia · US

Funding

Biotechnology and Biological Sciences Research Council BB/L023113/1British Heart Foundation IG/16/2/32273Cancer Research UK 12772Cancer Research UK 15182Cancer Research UK 17043Cancer Research UK 23302Cancer Research UK C14303/A17043Cancer Research UK C24461/A23303Cancer Research UK C25425/A15182Medical Research Council G0800021Medical Research Council MC_U105181009Medical Research Council MC_UP_A024_1008
6 · The paper itself

Abstract

Aurora-A regulates the recruitment of TACC3 to the mitotic spindle through a phospho-dependent interaction with clathrin heavy chain (CHC). Here, we describe the structural basis of these interactions, mediated by three motifs in a disordered region of TACC3. A hydrophobic docking motif binds to a previously uncharacterized pocket on Aurora-A that is blocked in most kinases. Abrogation of the docking motif causes a delay in late mitosis, consistent with the cellular distribution of Aurora-A complexes. Phosphorylation of Ser558 engages a conformational switch in a second motif from a disordered state, needed to bind the kinase active site, into a helical conformation. The helix extends into a third, adjacent motif that is recognized by a helical-repeat region of CHC, not a recognized phospho-reader domain. This potentially widespread mechanism of phospho-recognition provides greater flexibility to tune the molecular details of the interaction than canonical recognition motifs that are dominated by phosphate binding.

Indexed as

Aurora Kinase ACell LineHumansMicrotubule-Associated ProteinsProtein Conformation, alpha-HelicalSpindle ApparatusAurora Kinase AMicrotubule-Associated ProteinsTACC3 protein, humandisorder–order transitionintrinsically disordered proteinphosphorylationprotein kinaseprotein–protein interaction

Identifiers

PMID29510984
PMCPMC5897774
OpenAlexW2787878485

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.