Evidence map›Paper›PMID 26644180›Full record

ArticleJournal of cell science2016

Reactive oxygen species exert opposite effects on Tyr23 phosphorylation of the nuclear and cortical pools of annexin A2.

Ann Kari Grindheim, Hanne Hollås, Aase M Raddum, Jaakko Saraste, Anni Vedeler

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  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. Article
  9. Annexin A2 in Fibrinolysis, Inflammation and Fibrosis.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. ANXA2 promotes esophageal cancer progression by activating MYC-HIF1A-VEGF axis.Journal of experimental & clinical cancer research : CR · 2018
    Article
  14. Review
  15. Article
  16. 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

5 authors at 1 institution in 1 country.

Ann Kari GrindheimDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway Molecular Imaging Center (MIC), University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway.
Hanne HollåsDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway.
Aase M RaddumDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway.
Jaakko SarasteDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway Molecular Imaging Center (MIC), University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway.
Anni VedelerDepartment of Biomedicine, University of Bergen, Jonas Lies vei 91, Bergen N-5009, Norway Anni.Vedeler@biomed.uib.no.
University of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Annexin A2 (AnxA2) is a multi-functional and -compartmental protein whose subcellular localisation and functions are tightly regulated by its post-translational modifications. AnxA2 and its Tyr23-phosphorylated form (pTyr23AnxA2) are involved in malignant cell transformation, metastasis and angiogenesis. Here, we show that H2O2 exerts rapid, simultaneous and opposite effects on the Tyr23 phosphorylation status of AnxA2 in two distinct compartments of rat pheochromocytoma (PC12) cells. Reactive oxygen species induce dephosphorylation of pTyr23AnxA2 located in the PML bodies of the nucleus, whereas AnxA2 associated with F-actin at the cell cortex is Tyr23 phosphorylated. The H2O2-induced responses in both compartments are transient and the pTyr23AnxA2 accumulating at the cell cortex is subsequently incorporated into vesicles and then released to the extracellular space. Blocking nuclear export by leptomycin B does not affect the nuclear pool of pTyr23AnxA2, but increases the amount of total AnxA2 in this compartment, indicating that the protein might have several functions in the nucleus. These results suggest that Tyr23 phosphorylation can regulate the function of AnxA2 at distinct subcellular sites.

Indexed as

Protein Processing, Post-TranslationalActinsAnimalsAnnexin A2Cell MembraneCell NucleusExtracellular VesiclesHydrogen PeroxideOxidative StressPC12 CellsPhosphorylationProtein TransportRatsReactive Oxygen SpeciesTyrosineActinsAnnexin A2Hydrogen PeroxideReactive Oxygen SpeciesTyrosineAnnexin A2Cell cortexNucleusOxidative stressTyrosine phosphorylation

Identifiers

PMID26644180
PMCPMC4732284
OpenAlexW2394636836

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.