Evidence map›Paper›PMID 22357620›Full record

ArticleMolecular biology of the cell2012

Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres.

Ewa Niedzialkowska, Fangwei Wang, Przemyslaw J Porebski, Wladek Minor, Jonathan M G Higgins, P Todd Stukenberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023
    Article
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  9. Article
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  12. Article
  13. Review
  14. Review
  15. 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

6 authors at 3 institutions in 2 countries.

Ewa NiedzialkowskaDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.
Fangwei Wang
Przemyslaw J Porebski
Wladek Minor
Jonathan M G Higgins
P Todd Stukenberg
University of Virginia · USBrigham and Women's Hospital · USJagiellonian University · PL

Funding

X-RAY CRYSTALLOGRAPHY OF MACROMOLECULESR01GM053163 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MINOR, WLADEK, OTWINOWSKI, ZBYSZEK · 1996 to 2014
$6.3M
Dissection of the Inner Centromere Regulatory NetworkR01GM063045 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BEKIRANOV, STEFAN, STUKENBERG, P. TODD · 2001 to 2013
$4.0M
Function of the chromosomal kinase haspin in mitosisR01GM074210 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HIGGINS, JONATHAN M · 2006 to 2010
$1.6M
Mechanisms of "End On" Microtubule Attachment by the KinetochoreR01GM081576 · NIGMS · UNIVERSITY OF VIRGINIA · PI STUKENBERG, P. TODD · 2008 to 2011
$1.2M
NIGMS NIH HHS GM053163NIGMS NIH HHS R01 GM053163NIGMS NIH HHS R01 GM063045NIGMS NIH HHS R01GM063045NIGMS NIH HHS R01 GM074210NIGMS NIH HHS R01GM074210NIGMS NIH HHS R01 GM081576NIGMS NIH HHS R01GM081576
6 · The paper itself

Abstract

Survivin, a subunit of the chromosome passenger complex (CPC), binds the N-terminal tail of histone H3, which is phosphorylated on T3 by Haspin kinase, and localizes the complex to the inner centromeres. We used x-ray crystallography to determine the residues of Survivin that are important in binding phosphomodified histone H3. Mutation of amino acids that interact with the histone N-terminus lowered in vitro tail binding affinity and reduced CPC recruitment to the inner centromere in cells, validating our solved structures. Phylogenetic analysis shows that nonmammalian vertebrates have two Survivin paralogues, which we name class A and B. A distinguishing feature of these paralogues is an H-to-R change in an amino acid that interacts with the histone T3 phosphate. The binding to histone tails of the human class A paralogue, which has a histidine at this position, is sensitive to changes around physiological pH, whereas Xenopus Survivin class B is less so. Our data demonstrate that Survivin paralogues have different characteristics of phosphospecific binding to threonine-3 of histone H3, providing new insight into the biology of the inner centromere.

Indexed as

Amino Acid SequenceCell Line, TumorCentromereHeLa CellsHistonesHumansInhibitor of Apoptosis ProteinsPhosphorylationProtein Structure, TertiarySequence AlignmentSurvivinBIRC5 protein, humanHistonesInhibitor of Apoptosis ProteinsSurvivin

Identifiers

PMID22357620
PMCPMC3327328
OpenAlexW2139516530

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.