Evidence map›Paper›PMID 11360177›Full record

ArticleOncogene2001

Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction.

K Kurokawa, T Iwashita, H Murakami, H Hayashi, K Kawai, M Takahashi

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. FGF-based drug discovery: advances and challenges.Nature reviews. Drug discovery · 2025
    Review
  3. CCDC6-RET fusion protein regulates Ras/MAPK signaling through the fusion- GRB2-SHC1 signal niche.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. RET receptor signaling: Function in development, metabolic disease, and cancer.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Mitogen-Activated Protein (MAP) Kinase Scaffolding Proteins: A Recount.International journal of molecular sciences · 2013
    Article
  18. Structure and physiology of the RET receptor tyrosine kinase.Cold Spring Harbor perspectives in biology · 2013
    Review
  19. Article
  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

6 authors at 1 institution in 1 country.

K KurokawaDepartment of Pathology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan.
T Iwashita
H Murakami
H Hayashi
K Kawai
M Takahashi
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SNT/FRS2 is a lipid anchored docking protein that contains an amino-terminal myristylation signal, followed by a phosphotyrosine-binding (PTB) domain and a carboxy-terminal region with multiple tyrosine residues. Here we show that the SNT/FRS2 PTB domain binds to RET receptor tyrosine kinase activated by glial cell line-derived neurotrophic factor (GDNF) or multiple endocrine neoplasia (MEN) 2 mutations. Analyses by site directed-mutagenesis revealed that it binds to tyrosine 1062 in RET that is also known to be a binding site for the SHC adaptor protein. Whereas SHC bound to RET was associated with GRB2 and GAB1 proteins, SNT/FRS2 was associated with GRB2 only, suggesting that SNT/FRS2 is involved mainly in the activation of the RAS/mitogen activated protein kinase (MAPK) pathway but not the phosphatidylinositol 3-kinase (PI3-K)/AKT pathway. In addition, phosphorylated SNT/FRS2 appeared to directly complex with SHP-2 tyrosine phosphatase. These results suggest that tyrosine 1062 in RET provides a site for the interaction of multiple signaling molecules and that the balance of SHC and SNT/FRS2 binding may affect the nature of the intracellular signaling for cell proliferation, differentiation and survival induced by activated RET.

Indexed as

Adaptor Proteins, Signal TransducingDrosophila ProteinsNerve Growth Factors3T3 CellsAmino Acid SequenceAnimalsBinding SitesGlial Cell Line-Derived Neurotrophic FactorGlial Cell Line-Derived Neurotrophic Factor ReceptorsGRB2 Adaptor ProteinHumansIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMiceMolecular Sequence DataAdaptor Proteins, Signal TransducingDrosophila ProteinsFRS2 protein, humanGDNF protein, humanGdnf protein, mouseGlial Cell Line-Derived Neurotrophic FactorGlial Cell Line-Derived Neurotrophic Factor ReceptorsGRB2 Adaptor ProteinGRB2 protein, humanGrb2 protein, mouseIntracellular Signaling Peptides and ProteinsMembrane ProteinsNerve Growth FactorsNerve Tissue ProteinsPhosphoproteinsProtein IsoformsProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProto-Oncogene ProteinsProto-Oncogene Proteins c-retPTPN11 protein, humanPtpn11 protein, mousePTPN6 protein, humanPtpn6 protein, mouseReceptor Protein-Tyrosine KinasesRet protein, DrosophilaRet protein, mouseTyrosine

Identifiers

PMID11360177
OpenAlexW2315338108

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.