Evidence map›Paper›PMID 19665973›Full record

ArticleCell2009

The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.

Jae Hyun Bae, Erin Denise Lew, Satoru Yuzawa, Francisco Tomé, Irit Lax, Joseph Schlessinger

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

90 citing papers in PubMed, 157 citations in OpenAlex.

  1. Review
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  8. Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Lipid Binding of SH2 Domains.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

30 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 1 institution in 1 country.

Jae Hyun BaeDepartment of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
Erin Denise Lew
Satoru Yuzawa
Francisco Tomé
Irit Lax
Joseph Schlessinger
Yale University · US

Funding

Research Core: Biochemistry and histology/histomorphometryP50AR054086 · NIAMS · YALE UNIVERSITY · PI DEMAY, MARIE · 2006 to 2010
$8.5M
Docking protein FRS2 in FGF signalingR01AR051448 · NIAMS · YALE UNIVERSITY · PI SCHLESSINGER, JOSEPH · 2004 to 2008
$1.7M
FGF RECEPTOR SIGNALING IN BONE DEVELOPMENTR01AR051886 · NIAMS · YALE UNIVERSITY · PI SCHLESSINGER, JOSEPH · 2005 to 2009
$1.7M
NIAMS NIH HHS P50 AR054086NIAMS NIH HHS P50-AR054086NIAMS NIH HHS R01 AR051448NIAMS NIH HHS R01-AR051448NIAMS NIH HHS R01 AR051886NIAMS NIH HHS R01-AR051886
6 · The paper itself

Abstract

SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. However, the modest binding affinity of SH2 domains to pY containing peptides may not account for and likely represents an oversimplified mechanism for regulation of selectivity of signaling pathways in living cells. Here we describe the crystal structure of the activated tyrosine kinase domain of FGFR1 in complex with a phospholipase Cgamma fragment. The structural and biochemical data and experiments with cultured cells show that the selectivity of phospholipase Cgamma binding and signaling via activated FGFR1 are determined by interactions between a secondary binding site on an SH2 domain and a region in FGFR1 kinase domain in a phosphorylation independent manner. These experiments reveal a mechanism for how SH2 domain selectivity is regulated in vivo to mediate a specific cellular process.

Indexed as

Amino Acid SequenceAnimalsHumansMiceModels, MolecularMolecular Sequence DataPhosphotyrosineReceptor, Fibroblast Growth Factor, Type 1Sequence AlignmentSignal Transductionsrc Homology DomainsFGFR1 protein, humanFgfr1 protein, mousePhosphotyrosineReceptor, Fibroblast Growth Factor, Type 1

Identifiers

PMID19665973
PMCPMC4764080
OpenAlexW2160284078

What OpenQuestion holds

Textmetadata
LicenceTDM
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.