Evidence map›Paper›PMID 8628319›Full record

ArticleMolecular and cellular biology1996

The Drosophila insulin receptor activates multiple signaling pathways but requires insulin receptor substrate proteins for DNA synthesis.

L Yenush, R Fernandez, M G Myers, T C Grammer, X J Sun, J Blenis, J H Pierce, J Schlessinger, M F White

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Biochemical characterization of the Drosophila insulin receptor kinase and longevity-associated mutants.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Insects as a New Complex Model in Hormonal Basis of Obesity.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Genetic control of size in Drosophila.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2000
    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

9 authors at 5 institutions in 1 country.

L YenushResearch Division, Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
R Fernandez
M G Myers
T C Grammer
X J Sun
J Blenis
J H Pierce
J Schlessinger
M F White
Harvard University · USJoslin Diabetes Center · USColumbia University Irving Medical Center · USNational Institutes of Health · USNew York University · US

Funding

ONCOGENIC REGULATION OF S6 PROTEIN KINASE &CELL GROWTHR01CA046595 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI JOHN BLENIS · 1988 to 2026
$10.6M
Mitogenic and Oncogenic Regulation of ERK/RSK SignalingR37CA046595 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BLENIS, JOHN · 2003 to 2012
$6.4M
Regulating IRS-proteins by Ser/Thr PhosphorylationR01DK038712 · NIDDK · JOSLIN DIABETES CENTER · PI WHITE, MORRIS F. · 1992 to 2014
$5.0M
STRUCTURE AND FUNCTION OF THE IRS SIGNALING SYSTEMR01DK043808 · NIDDK · JOSLIN DIABETES CENTER · PI WHITE, MORRIS F. · 1991 to 2004
$1.7M
INSULIN RECEPTOR REGULATION BY MULTISITE PHOSPHORYLATIONR29DK038712 · NIDDK · JOSLIN DIABETES CENTER · PI WHITE, MORRIS F. · 1987 to 1989
–
INTERACTION BETWEEN INSULIN RECEPTORS AND CELL PROTEINSR55DK038712 · NIDDK · JOSLIN DIABETES CENTER · PI WHITE, MORRIS F. · 1991 to 1991
–
NCI NIH HHS CA46595NIDDK NIH HHS DK38712NIDDK NIH HHS DK43808
6 · The paper itself

Abstract

The Drosophila insulin receptor (DIR) contains a 368-amino-acid COOH-terminal extension that contains several tyrosine phosphorylation sites in YXXM motifs. This extension is absent from the human insulin receptor but resembles a region in insulin receptor substrate (IRS) proteins which binds to the phosphatidylinositol (PI) 3-kinase and mediates mitogenesis. The function of a chimeric DIR containing the human insulin receptor binding domain (hDIR) was investigated in 32D cells, which contain few insulin receptors and no IRS proteins. Insulin stimulated tyrosine autophosphorylation of the human insulin receptor and hDIR, and both receptors mediated tyrosine phosphorylation of Shc and activated mitogen-activated protein kinase. IRS-1 was required by the human insulin receptor to activate PI 3-kinase and p70s6k, whereas hDIR associated with PI 3-kinase and activated p70s6k without IRS-1. However, both receptors required IRS-1 to mediate insulin-stimulated mitogenesis. These data demonstrate that the DIR possesses additional signaling capabilities compared with its mammalian counterpart but still requires IRS-1 for the complete insulin response in mammalian cells.

Indexed as

Signal TransductionAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell LineDNADrosophila melanogasterEnzyme ActivationHumansInsulinInsulin Receptor Substrate ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationCalcium-Calmodulin-Dependent Protein KinasesDNAInsulinInsulin Receptor Substrate ProteinsIRS1 protein, humanPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein Serine-Threonine KinasesReceptor, InsulinRecombinant ProteinsRibosomal Protein S6 KinasesThymidine

Identifiers

PMID8628319
PMCPMC231240
OpenAlexW1906478988

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.