Evidence map›Paper›PMID 37227118›Full record

ArticleeLife2023

The structural basis of the multi-step allosteric activation of Aurora B kinase.

Dario Segura-Peña, Oda Hovet, Hemanga Gogoi, Jennine Dawicki-McKenna, Stine Malene Hansen Wøien, Manuel Carrer, Ben E Black, Michele Cascella, Nikolina Sekulic

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

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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

9 authors at 3 institutions in 2 countries.

Dario Segura-PeñaCentre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, Faculty of Medicine, Oslo, Norway.ORCID 0000-0001-6695-1042
Oda HovetCentre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, Faculty of Medicine, Oslo, Norway.
Hemanga GogoiCentre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, Faculty of Medicine, Oslo, Norway.
Jennine Dawicki-McKennaDepartment of Biochemistry and Biophysics, Penn Center for Genome Integrity, Epigenetics Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States.
Stine Malene Hansen WøienCentre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, Faculty of Medicine, Oslo, Norway.
Manuel CarrerHylleraas Centre for Quantum Molecular Sciences, University of Oslo, Oslo, Norway.
Ben E BlackDepartment of Biochemistry and Biophysics, Penn Center for Genome Integrity, Epigenetics Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States.
Michele CascellaHylleraas Centre for Quantum Molecular Sciences, University of Oslo, Oslo, Norway.
Nikolina SekulicCentre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, Faculty of Medicine, Oslo, Norway.ORCID 0000-0002-8027-9114
Nord University · NOUniversity of Oslo · NOUniversity of Pennsylvania · US

Funding

Centromere identity, strength, and regulationR35GM130302 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ben E. Black · 2019 to 2026
$4.3M
Investigating the regulation of Aurora B levels at the centromereF32GM108360 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DAWICKI MCKENNA, JENNINE M · 2014 to 2015
$109k
NIGMS NIH HHS F32 GM108360NIGMS NIH HHS R35 GM130302
6 · The paper itself

Abstract

Aurora B, together with IN-box, the C-terminal part of INCENP, forms an enzymatic complex that ensures faithful cell division. The [Aurora B/IN-box] complex is activated by autophosphorylation in the Aurora B activation loop and in IN-box, but it is not clear how these phosphorylations activate the enzyme. We used a combination of experimental and computational studies to investigate the effects of phosphorylation on the molecular dynamics and structure of [Aurora B/IN-box]. In addition, we generated partially phosphorylated intermediates to analyze the contribution of each phosphorylation independently. We found that the dynamics of Aurora and IN-box are interconnected, and IN-box plays both positive and negative regulatory roles depending on the phosphorylation status of the enzyme complex. Phosphorylation in the activation loop of Aurora B occurs intramolecularly and prepares the enzyme complex for activation, but two phosphorylated sites are synergistically responsible for full enzyme activity.

Indexed as

MitosisAllosteric RegulationAmino Acid SequenceAurora Kinase BCell DivisionPhosphorylationAurora Kinase BallosteryAurora Bautoactivationbiochemistrycell divisionchemical biologyconformational dynamicsE. colimolecular biophysicsprotein kinasestructural biologyxenopus

Identifiers

PMID37227118
PMCPMC10259393
OpenAlexW4378173382

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.