Evidence map›Paper›PMID 19129191›Full record

ArticleThe Journal of biological chemistry2009

The 48-kDa alternative translation isoform of PP2A:B56epsilon is required for Wnt signaling during midbrain-hindbrain boundary formation.

Zhigang Jin, Jianli Shi, Amit Saraf, Wenyan Mei, Guo-Zhang Zhu, Stefan Strack, Jing Yang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Review
  5. Article
  6. Role of protein phosphatase 2A in kidney disease (Review).Experimental and therapeutic medicine · 2021
    Review
  7. Article
  8. Article
  9. Therapeutic targeting of PP2A.The international journal of biochemistry & cell biology · 2018
    Review
  10. Maternal Dead-end 1 promotes translation ofDevelopment (Cambridge, England) · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
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  20. Review
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 3 institutions in 1 country.

Zhigang JinCenter for Cell and Development Biology, the Research Institute at Nationwide Children's Hospital, Department of Pediatrics, Ohio State University, Columbus, Ohio 43205, USA.
Jianli Shi
Amit Saraf
Wenyan Mei
Guo-Zhang Zhu
Stefan Strack
Jing Yang
Nationwide Children's Hospital · USUniversity of Iowa · USMarshall University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alternative translation is an underappreciated post-transcriptional regulation mechanism. Although only a small number of genes are found to be alternatively translated, most genes undergoing alternative translation play important roles in tumorigenesis and development. Protein phosphatase 2A (PP2A) is involved in many cellular events during tumorigenesis and development. The specificity, localization, and activity of PP2A are regulated by B regulatory subunits. B56epsilon, a member of the B56 regulatory subunit family, is involved in multiple signaling pathways and regulates a number of developmental processes. Here we report that B56epsilon is alternatively translated, leading to the production of a full-length form and a shorter isoform that lacks the N-terminal 76 amino acid residues of the full-length form. Alternative translation of B56epsilon occurs through a cap-dependent mechanism. We provide evidence that the shorter isoform is required for Wnt signaling and regulates the midbrain/hindbrain boundary formation during Xenopus embryonic development. This demonstrates that the shorter isoform of B56epsilon has important biological functions. Furthermore, we show that the N-terminal sequence of B56epsilon, which is not present in the shorter isoform, contains a nuclear localization signal, whereas the C terminus of B56epsilon contains a nuclear export signal. The shorter isoform, which lacks the N-terminal nuclear localization signal, is restricted to the cytoplasm. In contrast, the full-length form can be localized to the nucleus in a cell type-specific manner. The finding that B56epsilon is alternatively translated adds a new level of regulation to PP2A holoenzymes.

Indexed as

Active Transport, Cell NucleusAnimalsCell LineCell NucleusDrosophila melanogasterDrosophila ProteinsHoloenzymesHumansIsoenzymesMesencephalonMiceNuclear Localization SignalsPhosphoprotein PhosphatasesProtein BiosynthesisProtein Phosphatase 2Protein Structure, TertiaryDrosophila ProteinsHoloenzymesIsoenzymesNuclear Localization SignalsPhosphoprotein PhosphatasesPPP2CA protein, humanProtein Phosphatase 2RNA Capstws protein, DrosophilaWnt ProteinsXenopus Proteins

Identifiers

PMID19129191
PMCPMC2652268
OpenAlexW2050703700

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.