Evidence map›Paper›PMID 19121999›Full record

ArticleThe Journal of biological chemistry2009

PHAPI/pp32 suppresses tumorigenesis by stimulating apoptosis.

Wei Pan, Li S da Graca, Yufang Shao, Qian Yin, Hao Wu, Xuejun Jiang

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Gga-miR-181a modulates ANP32A expression and inhibits MDCC-MSB-1 cell.In vitro cellular & developmental biology. Animal · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. High-resolution crystal structure of the leucine-rich repeat domain of the human tumour suppressor PP32A (ANP32A).Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  9. Article
  10. Article
  11. Cracking the ANP32 whips: important functions, unequal requirement, and hints at disease implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Acidic nuclear phosphoprotein 32kDa (ANP32)B-deficient mouse reveals a hierarchy of ANP32 importance in mammalian development.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  18. CXCL12-mediated regulation of ANP32A/Lanp, a component of the inhibitor of histone acetyl transferase (INHAT) complex, in cortical neurons.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2011
    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 2 institutions in 1 country.

Wei PanCell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Li S da Graca
Yufang Shao
Qian Yin
Hao Wu
Xuejun Jiang
Memorial Sloan Kettering Cancer Center · USCornell University · US

Funding

Structural Studies of TNF Receptor Associated Factors (TRAFs)R01AI045937 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI WU, HAO · 1999 to 2016
$5.9M
Molecular Regulation of Apoptosome ActivityR01CA113890 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI JIANG, XUEJUN · 2006 to 2010
$1.4M
NCI NIH HHS R01 CA113890NIAID NIH HHS R01 AI045937
6 · The paper itself

Abstract

PHAPI/pp32 is a tumor suppressor whose expression is altered in various human cancers. Although PHAPI possesses multiple biochemical activities, the molecular basis for its tumor-suppressive function has remained obscure. Recently we identified PHAPI as an apoptotic enhancer that stimulates apoptosome-mediated caspase activation. In this study, we defined the structural requirement for its activity to stimulate caspase activation using a series of truncation mutants of PHAPI. Further, utilizing these mutants, we provide evidence to support the model that the apoptotic activity of PHAPI is required for its tumor-suppressive capability. Consistently, pp32R1, a close homolog of PHAPI and yet an oncoprotein, is not able to stimulate caspase activation. A highly discrete region between these two proteins localizes to an essential caspase activation motif of PHAPI. Additionally, PHAPI is predominantly a nuclear protein, and it can translocate to the cytoplasm during apoptosis. Disruption of the nuclear localization signal of PHAPI caused a modest decrease of its tumor-suppressive function, indicating that nuclear localization of PHAPI contributes to, but is not essential for, tumor suppression.

Indexed as

ApoptosisAmino Acid MotifsAnimalsApoptosis Inducing FactorCaspasesCell NucleusCell Transformation, NeoplasticEnzyme ActivationHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMiceMutationNuclear Localization SignalsNuclear ProteinsPhosphoproteinsANP32A protein, humanApoptosis Inducing FactorCaspasesIntracellular Signaling Peptides and ProteinsNuclear Localization SignalsNuclear ProteinsPhosphoproteinsRNA-Binding ProteinsTumor Suppressor Proteins

Identifiers

PMID19121999
PMCPMC2652289
OpenAlexW1985214922

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.