Evidence map›Paper›PMID 9307968›Full record

ArticleMolecular biology of the cell1997

Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells.

H Y She, S Rockow, J Tang, R Nishimura, E Y Skolnik, M Chen, B Margolis, W Li

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. 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
4.8field-weighted citation impact, top 4% 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, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Allosteric N-WASP activation by an inter-SH3 domain linker in Nck.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Article
  7. Review
  8. Article
  9. Models for actin polymerization motors.Journal of mathematical biology · 2009
    Review
  10. Review
  11. Grb2 signaling in cell motility and cancer.Expert opinion on therapeutic targets · 2008
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

8 authors at 1 institution in 1 country.

H Y SheBen May Institute for Cancer Research, University of Chicago, Illinois 60637, USA.
S Rockow
J Tang
R Nishimura
E Y Skolnik
M Chen
B Margolis
W Li
May Institute · US

Funding

STUDIES OF A NOVEL SH2/SH3-CONTAINING CELLULAR ONCOGENER01CA065567 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LI, WEI · 1995 to 1999
–
NCI NIH HHS R01CA65567-01A1
6 · The paper itself

Abstract

Src homology domains [i.e., Src homology domain 2 (SH2) and Src homology domain 3 (SH3)] play a critical role in linking receptor tyrosine kinases to downstream signaling networks. A well-defined function of the SH3-SH2-SH3 adapter Grb2 is to link receptor tyrosine kinases, such as the epidermal growth factor receptor (EGFR), to the p21ras-signaling pathway. Grb2 has also been implicated to play a role in growth factor-regulated actin assembly and receptor endocytosis, although the underlying mechanisms remain unclear. In this study, we show that Grb2 interacts through its SH3 domains with the human Wiskott-Aldrich syndrome protein (WASp), which plays a role in regulation of the actin cytoskeleton. We find that WASp is expressed in a variety of cell types and is exclusively cytoplasmic. Although the N-terminal SH3 domain of Grb2 binds significantly stronger than the C-terminal SH3 domain to WASp, full-length Grb2 shows the strongest binding. Both phosphorylation of WASp and its interaction with Grb2, as well as with another adapter protein Nck, remain constitutive in serum-starved or epidermal growth factor-stimulated cells. WASp coimmunoprecipitates with the activated EGFR after epidermal growth factor stimulation. Purified glutathione S-transferase-full-length-Grb2 fusion protein, but not the individual domains of Grb2, enhances the association of WASp with the EGFR, suggesting that Grb2 mediates the association of WASp with EGFR. This study suggests that Grb2 translocates WASp from the cytoplasm to the plasma membrane and the Grb2-WASp complex may play a role in linking receptor tyrosine kinases to the actin cytoskeleton.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell LineErbB ReceptorsGRB2 Adaptor ProteinHematopoietic Stem CellsKidneyMiceOncogene ProteinsPrecipitin TestsProtein BindingProtein BiosynthesisProteinssrc Homology DomainsTumor Cells, CulturedWiskott-Aldrich SyndromeAdaptor Proteins, Signal TransducingErbB ReceptorsGRB2 Adaptor ProteinGrb2 protein, mouseNck proteinOncogene ProteinsProteinsWas protein, mouseWiskott-Aldrich Syndrome Protein

Identifiers

PMID9307968
PMCPMC305731
OpenAlexW2076808220

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.