Evidence map›Paper›PMID 15197263›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Control of cell size through phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol 3-kinase.

Robert Drakas, Xiao Tu, Renato Baserga

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 81 citations in OpenAlex.

  1. Trial
  2. Therapeutic advances of targeting receptor tyrosine kinases in cancer.Signal transduction and targeted therapy · 2024
    Review
  3. Article
  4. PI3Kα Translocation Mediates Nuclear PtdIns(3,4,5)PMolecular & cellular proteomics : MCP · 2023
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Nuclear PI3K signaling in cell growth and tumorigenesis.Frontiers in cell and developmental biology · 2015
    Review
  14. Review
  15. Article
  16. Nuclear IRS-1 and cancer.Journal of cellular physiology · 2012
    Review
  17. Review
  18. Article
  19. Review
  20. 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

3 authors at 2 institutions in 1 country.

Robert DrakasKimmel Cancer Center, Thomas Jefferson University, 233 South 10th Street, 624 Bluemle Life Sciences Building, Philadelphia, PA 19107, USA.
Xiao Tu
Renato Baserga
Thomas Jefferson University · USSidney Kimmel Cancer Center · US

Funding

A Role of the IGF-1 Receptor In AgingR01AG020956 · NIA · THOMAS JEFFERSON UNIVERSITY · PI BASERGA, RENATO LUIGI · 2001 to 2005
$1.5M
REGULATION OF CELL PROLIFERATION BY GENES OF THE MYB FAMILYP01CA056309 · NCI · THOMAS JEFFERSON UNIVERSITY · PI GIORDANO, ANTONIO · 1991 to 2001
$1.4M
NCI NIH HHS CA56309NIA NIH HHS AG20956NIA NIH HHS R01 AG020956
6 · The paper itself

Abstract

The insulin-like growth factor I/insulin receptor substrate 1 axis controls, in a nonredundant way, approximately 50% of cell and body size in animals from Drosophila to mice and in cells in culture. Although other factors may also intervene, cell size is strongly dependent on ribosome biogenesis, which is under the control of RNA polymerase I activity. We have previously shown that insulin receptor substrate 1 (IRS-1) translocates to the nuclei and nucleoli, where it binds to the upstream binding factor (UBF) 1, a regulator of RNA polymerase I activity. Activation of UBF1 requires its phosphorylation. However, IRS-1 is not a kinase, and we searched for an intermediate kinase that can phosphorylate UBF1. We demonstrate here that IRS-1 binds also to the phosphatidylinositol 3-kinase (PI3-K) subunits in nuclear extracts, and that the p110 subunit of PI3-K directly phosphorylates and activates UBF1, an exclusively nucleolar protein. The interaction of IRS-1, PI3-K, and UBF1 in the nucleoli provides one of the mechanisms for the effects of IRS-1 on cell and body size.

Indexed as

3T3 CellsAnimalsCell LineCell NucleusCell SizeChromonesEnzyme InhibitorsHigh Mobility Group ProteinsKineticsMiceMorpholinesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationPol1 Transcription Initiation Complex Proteins2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneChromonesEnzyme InhibitorsHigh Mobility Group ProteinsMorpholinesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPol1 Transcription Initiation Complex Proteinstranscription factor UBF

Identifiers

PMID15197263
PMCPMC438966
OpenAlexW2056950301

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.