Evidence map›Paper›PMID 23715859›Full record

ArticleCellular and molecular life sciences : CMLS2014

The tumor suppressor annexin A10 is a novel component of nuclear paraspeckles.

Nina Quiskamp, Michaela Poeter, Carsten Alexander Raabe, Ulli Martin Hohenester, Simone König, Volker Gerke, Ursula Rescher

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Annexin, a Protein for All Seasons: From Calcium Dependent Membrane Metabolism to RNA Recognition.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  2. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
  3. Article
  4. RNA-binding is an ancient trait of the Annexin family.Frontiers in cell and developmental biology · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Annexin Animal Models-From Fundamental Principles to Translational Research.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Annexins in Translational Research: Hidden Treasures to Be Found.International journal of molecular sciences · 2018
    Review
  11. Functional Association between Regulatory RNAs and the Annexins.International journal of molecular sciences · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Annexin A10 is a marker for the serrated pathway of colorectal carcinoma.Virchows Archiv : an international journal of pathology · 2015
    Article
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

7 authors at 1 institution in 1 country.

Nina QuiskampInstitute of Medical Biochemistry, Centre for Molecular Biology of Inflammation, and Interdisciplinary Clinical Research Centre, University of Münster, 48149, Münster, Germany.
Michaela Poeter
Carsten Alexander Raabe
Ulli Martin Hohenester
Simone König
Volker Gerke
Ursula Rescher
University of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Annexin A10 is the latest identified member of the annexin family of Ca(2+)- and phospholipid-binding proteins. In previous studies, downregulation of annexin A10 was correlated with dedifferentiation, invasion, and tumor progression, pointing to a possible tumor suppressor role. However, the biochemical characteristics and functions of annexin A10 remain unknown. We show that annexin A10 displays biochemical characteristics atypical for an annexin, indicating a Ca(2+)- and membrane-binding-independent function. Annexin A10 co-localizes with the mRNA-binding proteins SFPQ and PSPC1 at paraspeckles, an only recently discovered nuclear body, and decreases paraspeckle numbers when overexpressed in HeLa cells. In addition, annexin A10 relocates to dark perinucleolar caps upon transcriptional inhibition of RNA polymerase II. We mapped the cap-binding function of annexin A10 to the proximal part of the core domain, which is missing in the short isoform of annexin A10, and show its independence from the remaining functional type II Ca(2+)-binding site. In contrast to this, paraspeckle recruitment required additional core regions and was negatively affected by the mutation of the last type II Ca(2+)-binding site. Additionally, we show that overexpression of annexin A10 in HeLa cells increases their sensitivity to apoptosis and reduces colony formation. The identification of unique nuclear and biochemical characteristics of annexin A10 points towards its membrane-independent role in paraspeckle-associated mRNA regulation or processing.

Indexed as

AnimalsAnnexinsAntibiotics, AntineoplasticApoptosisCalciumCell NucleusDogsDoxorubicinHeLa CellsHumansMadin Darby Canine Kidney CellsNuclear ProteinsProtein IsoformsPTB-Associated Splicing FactorRNA-Binding ProteinsRNA, MessengerAnnexinsAntibiotics, AntineoplasticANXA10 protein, humanCalciumDoxorubicinNuclear ProteinsProtein IsoformsPSPC1 protein, humanPTB-Associated Splicing FactorRNA-Binding ProteinsRNA, MessengerRNA Polymerase II

Identifiers

PMID23715859
PMCPMC11113197
OpenAlexW2159080320

What OpenQuestion holds

Textmetadata
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.