Evidence map›Paper›PMID 15611341›Full record

ArticleThe Journal of cell biology2004

Palmitoylation supports assembly and function of integrin-tetraspanin complexes.

Xiuwei Yang, Oleg V Kovalenko, Wei Tang, Christoph Claas, Christopher S Stipp, Martin E Hemler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

112 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
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  10. Article
  11. Arabidopsis Tetraspanins Facilitate Virus InfectionFrontiers in plant science · 2022
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.International journal of molecular sciences · 2020
    Review
  19. Review
  20. Article

52 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 2 institutions in 1 country.

Xiuwei YangDana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Oleg V Kovalenko
Wei Tang
Christoph Claas
Christopher S Stipp
Martin E Hemler
Dana-Farber Cancer Institute · USHarvard University · US

Funding

Support of carcinoma metastasis by integrin a6-CD151-PKC complexesR01CA042368 · NCI · DANA-FARBER CANCER INSTITUTE · PI HEMLER, MARTIN E · 1986 to 2019
$5.4M
NOVEL INTEGRIN-CD151-PKC SIGNALING COMPLEXR01CA086712 · NCI · DANA-FARBER CANCER INSTITUTE · PI HEMLER, MARTIN E · 2000 to 2004
$1.6M
NCI NIH HHS CA42368NCI NIH HHS CA86712NCI NIH HHS R01 CA042368NCI NIH HHS R01 CA086712
6 · The paper itself

Abstract

As observed previously, tetraspanin palmitoylation promotes tetraspanin microdomain assembly. Here, we show that palmitoylated integrins (alpha3, alpha6, and beta4 subunits) and tetraspanins (CD9, CD81, and CD63) coexist in substantially overlapping complexes. Removal of beta4 palmitoylation sites markedly impaired cell spreading and signaling through p130Cas on laminin substrate. Also in palmitoylation-deficient beta4, secondary associations with tetraspanins (CD9, CD81, and CD63) were diminished and cell surface CD9 clustering was decreased, whereas core alpha6beta4-CD151 complex formation was unaltered. There is also a functional connection between CD9 and beta4 integrins, as evidenced by anti-CD9 antibody effects on beta4-dependent cell spreading. Notably, beta4 palmitoylation neither increased localization into "light membrane" fractions of sucrose gradients nor decreased solubility in nonionic detergents-hence it does not promote lipid raft association. Instead, palmitoylation of beta4 (and of the closely associated tetraspanin CD151) promotes CD151-alpha6beta4 incorporation into a network of secondary tetraspanin interactions (with CD9, CD81, CD63, etc.), which provides a novel framework for functional regulation.

Indexed as

AnimalsAntigens, CDCell LineHumansIntegrin beta3IntegrinsMacromolecular SubstancesMembrane GlycoproteinsMembrane MicrodomainsMembrane ProteinsPalmitic AcidProtein SubunitsReceptors, Growth Factorsrc-Family KinasesTetraspanin 29Antigens, CDCD9 protein, humanIntegrin beta3IntegrinsMacromolecular SubstancesMembrane GlycoproteinsMembrane ProteinsPalmitic AcidProtein SubunitsReceptors, Growth Factorsrc-Family KinasesTetraspanin 29

Identifiers

PMID15611341
PMCPMC2172609
OpenAlexW2096477148

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.