Evidence map›Paper›PMID 10449753›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Leptin receptor activation of SH2 domain containing protein tyrosine phosphatase 2 modulates Ob receptor signal transduction.

C Li, J M Friedman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
8.9field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 175 citations in OpenAlex.

  1. Emerging role of leptin in rheumatoid arthritis.Clinical and experimental immunology · 2014
    Pooled it
  2. Role of Sam68 as an adaptor protein in inflammatory signaling.Cellular and molecular life sciences : CMLS · 2024
    Review
  3. Signaling pathways in obesity: mechanisms and therapeutic interventions.Signal transduction and targeted therapy · 2022
    Review
  4. Leptin signaling and leptin resistance.Medical review (2021) · 2022
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Incendiary Leptin.Nutrients · 2020
    Review
  11. Review
  12. Review
  13. Review
  14. The Leptin Receptor Complex: Heavier Than Expected?Frontiers in endocrinology · 2017
    Review
  15. Protein tyrosine phosphatase-1B contributes to LPS-induced leptin resistance in male rats.American journal of physiology. Endocrinology and metabolism · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Leptin signaling and leptin resistance.Frontiers of medicine · 2013
    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

2 authors at 1 institution in 1 country.

C LiHoward Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY, USA.
J M Friedman
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leptin exerts its weight-reducing effects by binding to its receptor and activating signal transduction in hypothalamic neurons and other cell types. To identify the components of the leptin signal transduction pathway, an approach was developed in which bacterially expressed phosphorylated fragments of Ob receptor b (Ob-Rb) were used as affinity agents. Leptin binding to the Ob-Rb form of the leptin receptor leads to tyrosyl phosphorylation of the cytoplasmic domain of its receptor. Two of the three cytoplasmic tyrosines of Ob-Rb, at positions 985 and 1138, are phosphorylated after leptin treatment. Affinity chromatography using a tyrosine-phosphorylated fragment spanning Tyr 985 of Ob-Rb was used to identify proteins that bind to this site. The SH2 domain containing protein tyrosine phosphatase 2 (SHP-2) was isolated from bovine and mouse hypothalamus by using this method. After cotransfection of Ob-Rb, Janus kinase 2 (JAK2), and SHP-2 into 293T cells, leptin results in direct binding of SHP-2 to the phosphorylated Tyr 985. The bound SHP-2 is itself tyrosine phosphorylated after leptin treatment. SHP-2 is not phosphorylated after leptin treatment when a Y-->F 985 receptor mutant is cotransfected. In the absence of SHP-2 phosphorylation, the level of JAK2 phosphorylation was increased. Tyrosyl phosphorylation of the leptin receptor and signal transducer and activater of transcription 3 (STAT3) are not affected by phosphorylation of SHP-2. These data suggest that activation of SHP-2 by the leptin receptor results in a decreased phosphorylation of JAK2 and may act to attenuate leptin signal transduction. The method used in this report can in principle be used to isolate additional components of the leptin, or other, signal transduction pathway.

Indexed as

Proto-Oncogene ProteinsReceptors, Cell SurfaceSignal TransductionAmino Acid SequenceAnimalsCarrier ProteinsCattleCell LineElectrophoresis, Polyacrylamide GelEnzyme ActivationIntracellular Signaling Peptides and ProteinsJanus Kinase 2MiceMolecular Sequence DataObesityProtein Phosphatase 2Carrier ProteinsIntracellular Signaling Peptides and ProteinsJak2 protein, mouseJanus Kinase 2leptin receptor, mouseProtein Phosphatase 2Protein-Tyrosine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProto-Oncogene ProteinsPtpn11 protein, mousePtpn6 protein, mouseReceptors, Cell SurfaceReceptors, LeptinSH2 Domain-Containing Protein Tyrosine Phosphatases

Identifiers

PMID10449753
PMCPMC22269
OpenAlexW2157273158

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.