Evidence map›Paper›PMID 20181947›Full record

ArticleThe Journal of biological chemistry2010

Interaction of syndecan and alpha6beta4 integrin cytoplasmic domains: regulation of ErbB2-mediated integrin activation.

Haiyao Wang, LuAnn Leavitt, Ravishankar Ramaswamy, Alan C Rapraeger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 66 citations in OpenAlex.

  1. SSTNSignal transduction and targeted therapy · 2026
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  5. PDZ scaffolds regulate extracellular vesicle production, composition, and uptake.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Review
  8. Review
  9. Heparan Sulfate Proteoglycan Signaling in Tumor Microenvironment.International journal of molecular sciences · 2020
    Review
  10. Review
  11. Tetraspanin-6 negatively regulates exosome production.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. The Cardiac Syndecan-2 Interactome.Frontiers in cell and developmental biology · 2020
    Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Haiyao WangDepartment of Pathology and Laboratory Medicine, University of Wisconsin, Madison, Wisconsin 53705, USA.
LuAnn Leavitt
Ravishankar Ramaswamy
Alan C Rapraeger
University of Wisconsin–Madison · US

Funding

Proteoglycans of the Plasma MembraneR01CA109010 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RAPRAEGER, ALAN C · 2004 to 2008
$1.2M
NCI NIH HHS R01 CA109010NCI NIH HHS R01-CA109010
6 · The paper itself

Abstract

The alpha6beta4 integrin is a laminin 332 (LN332) receptor central to the formation of hemidesmosomes in epithelial layers. However, the integrin becomes phosphorylated by keratinocytes responding to epidermal growth factor in skin wounds or by squamous cell carcinomas that overexpress/hyperactivate the tyrosine kinase ErbB2, epidermal growth factor receptor, or c-Met. We show here that the beta4-dependent signaling in A431 human squamous carcinoma cells is dependent on the syndecan family of matrix receptors. Yeast two-hybrid analysis identifies an interaction within the distal third (amino acids 1473-1752) of the beta4 cytoplasmic domain and the conserved C2 region of the syndecan cytoplasmic domain. Via its C2 region, Sdc1 forms a complex with the alpha6beta4 integrin along with the receptor tyrosine kinase ErbB2 and the cytoplasmic kinase Fyn in A431 cells. Engagement of LN332 or clustering of the alpha6beta4 integrin with integrin-specific antibodies causes phosphorylation of ErbB2, Fyn, and the beta4 subunit as well as activation of phosphatidylinositol 3-kinase and Akt and their assimilation into this complex. This leads to phosphatidylinositol 3-kinase-dependent cell spreading and Akt-dependent protection from apoptosis. This is disrupted by RNA interference silencing of Sdc1 but can be rescued by mouse Sdc1 or Sdc4 but not by syndecan mutants lacking their C-terminal C2 region. This disruption does not prevent the phosphorylation of ErbB2 or Fyn but blocks the Fyn-mediated phosphorylation of the beta4 tail. We propose that syndecans engage the distal region of the beta4 cytoplasmic domain and bring it to the plasma membrane, where it can be acted upon by Src family kinases.

Indexed as

AnimalsApoptosisCell LineEnzyme ActivationErb-b2 Receptor Tyrosine KinasesHemidesmosomesHumansIntegrin alpha6beta4KeratinocytesMiceMultiprotein ComplexesPhosphatidylinositol 3-KinasesPhosphorylationProtein Structure, TertiaryProto-Oncogene Proteins c-aktRatsERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesIntegrin alpha6beta4Multiprotein ComplexesPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktSDC1 protein, humanSDC4 protein, humanSyndecan-1Syndecan-4Syndecans

Identifiers

PMID20181947
PMCPMC2859518
OpenAlexW2048732928

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.