Evidence map›Paper›PMID 21193415›Full record

ArticleThe Journal of biological chemistry2011

Structure-function analysis of tetraspanin CD151 reveals distinct requirements for tumor cell behaviors mediated by α3β1 versus α6β4 integrin.

Shannin Zevian, Nicole E Winterwood, Christopher S Stipp

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Modulation of voltage-gated CaChannels (Austin, Tex.) · 2020
    Review
  7. Article
  8. CD151 in Respiratory Diseases.Frontiers in cell and developmental biology · 2020
    Review
  9. Integrin-independent support of cancer drug resistance by tetraspanin CD151.Cellular and molecular life sciences : CMLS · 2019
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Tetraspanins in cell migration.Cell adhesion & migration · 2015
    Review
  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

3 authors at 1 institution in 1 country.

Shannin ZevianDepartment of Biology, University of Iowa, Iowa City, Iowa 52242, USA.
Nicole E Winterwood
Christopher S Stipp
University of Iowa · US

Funding

Dissecting the opposing roles of alpha-3 integrin in metastasisR01CA136664 · NCI · UNIVERSITY OF IOWA · PI STIPP, CHRISTOPHER S. · 2009 to 2013
$1.5M
NCI NIH HHS CA136664NCI NIH HHS R01 CA136664
6 · The paper itself

Abstract

The basement membrane protein laminin-332 (laminin-5) mediates both stable cell adhesion and rapid cell migration and thus has the potential to either restrain or promote tumor cell metastasis. The major cellular receptors for laminin-332 are integrin α3β1, which mediates rapid tumor cell migration, and integrin α6β4, which often mediates stable cell attachment. Tetraspanin protein CD151 interacts directly with both α3β1 and α6β4 integrins and with other tetraspanins, thereby promoting α3β1 and α6β4 association with tetraspanin-enriched microdomains on the cell surface. To explore the possibility of selectively modulating tumor cell responses to laminin-332, we re-expressed a series of CD151 mutants in epidermoid carcinoma cells with near total, RNAi-mediated silencing of endogenous CD151. The interactions of CD151 with its integrin partners or its interactions with other tetraspanins were selectively disrupted by specific mutations in the CD151 large extracellular loop (EC2 domain) or in intracellular CD151 palmitoylation sites, respectively. CD151-integrin association and CD151-tetraspanin association were both important for α3β1 integrin-dependent initial adhesion and rapid migration on laminin-332. Remarkably, however, only CD151-integrin association was required for stable, α6β4 integrin-dependent cell attachment on laminin-332. In addition, we found that a QRD amino acid motif in the CD151 EC2 domain, which had been thought to be crucial for CD151-integrin interaction, is not essential for CD151-integrin association or for the ability of CD151 to promote several different integrin functions. These new data suggest potential strategies for selectively modulating migratory cell responses to laminin-332, while leaving stable cell attachment on laminin-332 intact.

Indexed as

Antigens, CDBasement MembraneCarcinoma, Squamous CellCell AdhesionCell Adhesion MoleculesCell Line, TransformedCell Line, TumorCell MovementHumansIntegrin alpha3beta1Integrin alpha6beta4KalininKeratinocytesLipoylationMutagenesisStructure-Activity RelationshipAntigens, CDCD151 protein, humanCell Adhesion MoleculesIntegrin alpha3beta1Integrin alpha6beta4KalininTetraspanin 24

Identifiers

PMID21193415
PMCPMC3045005
OpenAlexW2072388293

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.