Evidence map›Paper›PMID 21576258›Full record

ArticleGenes & development2011

mTOR phosphorylates IMP2 to promote IGF2 mRNA translation by internal ribosomal entry.

Ning Dai, Joseph Rapley, Matthew Angel, M Fatih Yanik, Michael D Blower, Joseph Avruch

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
–field-weighted citation impact
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

131 citing papers in PubMed, 210 citations in OpenAlex.

  1. Deltacoronavirus Modulates circRNA cGLIS3 Metabolism to Evade Host Antiviral Response.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Impact ofInternational journal of medical sciences · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. A circular RNA overcomes acquired resistance to BET inhibitors by antagonizing IGF2BP2-mediated c-MYC translation in TNBC.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. IGF2BP2: an mCellular & molecular biology letters · 2025
    Review
  19. IMPlications of IMP2 in RNA Biology and Disease.International journal of molecular sciences · 2025
    Review
  20. Article

71 more citing papers are in PubMed but not listed here.

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.

Ning DaiDepartment of Molecular Biology, Massachusetts General Hospital, Boston, USA.
Joseph Rapley
Matthew Angel
M Fatih Yanik
Michael D Blower
Joseph Avruch
Harvard University · USMassachusetts Institute of Technology · US

Funding

Pilot & Feasibility ProgramP30DK043351 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI RAYMOND T CHUNG · 1991 to 2026
$35.3M
Transgenic CoreP30DK057521 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI FLOREZ, JOSE CARLOS · 2000 to 2019
$31.4M
PHOSPHOPEPTIDE METABOLISM IN ADIPOCYTESR37DK017776 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI AVRUCH, JOSEPH · 1999 to 2018
$9.3M
MOLECULAR BASIS OF CELL GROWTH CONTROL BY THE TOR KINASER01CA073818 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI AVRUCH, JOSEPH · 1997 to 2011
$5.1M
NCI NIH HHS R01 CA073818NIDDK NIH HHS P30 DK043351NIDDK NIH HHS P30 DK057521NIDDK NIH HHS R37 DK017776
6 · The paper itself

Abstract

Variants in the IMP2 (insulin-like growth factor 2 [IGF2] mRNA-binding protein 2) gene are implicated in susceptibility to type 2 diabetes. We describe the ability of mammalian target of rapamycin (mTOR) to regulate the cap-independent translation of IGF2 mRNA through phosphorylation of IMP2, an oncofetal RNA-binding protein. IMP2 is doubly phosphorylated in a rapamycin-inhibitable, amino acid-dependent manner in cells and by mTOR in vitro. Double phosphorylation promotes IMP2 binding to the IGF2 leader 3 mRNA 5' untranslated region, and the translational initiation of this mRNA through eIF-4E- and 5' cap-independent internal ribosomal entry. Unexpectedly, the interaction of IMP2 with mTOR complex 1 occurs through mTOR itself rather than through raptor. Whereas depletion of mTOR strongly inhibits IMP2 phosphorylation in cells, comparable depletion of raptor has no effect; moreover, the ability of mTOR to phosphorylate IMP2 in vitro is unaffected by the elimination of raptor. Dual phosphorylation of IMP2 at the mTOR sites is evident in the mouse embryo, likely coupling nutrient sufficiency to IGF2 expression and fetal growth. Doubly phosphorylated IMP2 is also widely expressed in adult tissues, including islets of Langerhans.

Indexed as

Gene Expression Regulation5' Untranslated RegionsAdaptor Proteins, Signal TransducingAnimalsAnti-Bacterial AgentsCell LineHEK293 CellsHumansInsulin-Like Growth Factor IIMiceMutationPhosphorylationProtein BindingRegulatory-Associated Protein of mTORRibosomesRNA-Binding Proteins5' Untranslated RegionsAdaptor Proteins, Signal TransducingAnti-Bacterial AgentsIGF2BP2 protein, humanIGF2BP2 protein, mouseIGF2 protein, humanIGF2 protein, mouseInsulin-Like Growth Factor IIMTOR protein, humanRegulatory-Associated Protein of mTORRNA-Binding ProteinsRNA, MessengerRPTOR protein, humanSirolimusTOR Serine-Threonine Kinases

Identifiers

PMID21576258
PMCPMC3110954
OpenAlexW2130540738

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.