Evidence map›Paper›PMID 12789267›Full record

ArticleOncogene2003

v-Src induces Shc binding to tyrosine 63 in the cytoplasmic domain of the LDL receptor-related protein 1.

Helen Barnes, Elizabeth J Ackermann, Peter van der Geer

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. LRP-1: functions, signaling and implications in kidney and other diseases.International journal of molecular sciences · 2014
    Review
  8. Article
  9. Article
  10. Cell cholesterol modulates metalloproteinase-dependent shedding of low-density lipoprotein receptor-related protein-1 (LRP-1) and clearance function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

3 authors at 2 institutions in 1 country.

Helen BarnesDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0601, USA.
Elizabeth J Ackermann
Peter van der Geer
University of California, San Diego · USTorrey Pines Institute For Molecular Studies · US

Funding

HEMOGLOBIN AND BLOOD PROTEIN CHEMISTRYT32DK007233 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1986 to 2012
$4.6M
ROLE IN SHC IN NORMAL AND MALIGNANT SIGNAL TRANSDUCTIONR29CA078629 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI VAN DER GEER, PETER · 1998 to 2002
$330k
NCI NIH HHS R29 CA78629NIDDK NIH HHS DK 07233
6 · The paper itself

Abstract

We recently observed that the LDL receptor-related protein 1 (LRP-1) is tyrosine phosphorylated in v-Src-transformed cells. Using a GST-fusion protein containing the cytoplasmic domain of LRP-1, we show that LRP-1 is a direct substrate for v-Src in vitro. To study LRP-1 phosphorylation in vivo, we constructed an LRP-1 minireceptor composed of the beta chain linked at the amino-terminus to a Myc epitope (Myc-LRPbeta). When expressed together with v-Src, Myc-LRPbeta becomes phosphorylated on tyrosine. Of the four tyrosine residues present in the cytoplasmic domain of LRP-1, only Tyr 63 is phosphorylated by v-Src in vivo or in vitro. Using fibroblasts deficient in Src, Yes and Fyn, we were able to show that there are multiple kinases present in the cell that can phosphorylate LRP-1. Tyrosine-phosphorylated LRP-1 associates with Shc, a PTB and SH2 domain containing signaling protein that is involved in the activation of Ras. Binding of the purified Shc PTB domain to Tyr 63 containing peptides shows that the interaction between LRP-1 and Shc is direct. We found that DAB, a PTB domain containing signaling protein that is involved in signaling by LDL receptor-related proteins in the nervous system, did not bind to full-length LRP-1. Our observations suggest that LRP-1 may be involved in normal and malignant signal transduction through a direct interaction with Shc adaptor proteins.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCell Line, TransformedCells, CulturedCytoplasmEpitopesGenes, mycLow Density Lipoprotein Receptor-Related Protein-1Molecular Sequence DataMutationOncogene Protein pp60(v-src)PhosphorylationAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportEpitopesLow Density Lipoprotein Receptor-Related Protein-1Oncogene Protein pp60(v-src)ProteinsRecombinant Fusion ProteinsShc Signaling Adaptor ProteinsTyrosine

Identifiers

PMID12789267
OpenAlexW1983909864

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.