Evidence map›Paper›PMID 18195108›Full record

ArticleThe Journal of cell biology2008

Cytoskeleton assembly at endothelial cell-cell contacts is regulated by alphaII-spectrin-VASP complexes.

Peter M Benz, Constanze Blume, Jan Moebius, Chris Oschatz, Kai Schuh, Albert Sickmann, Ulrich Walter, Stephan M Feller, Thomas Renné

Abstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

59 citing papers in PubMed, 115 citations in OpenAlex.

  1. Mena, a new available marker in tumors of salivary glands?European journal of histochemistry : EJH · 2012
    Trial
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  12. The role of spectrin in cell adhesion and cell-cell contact.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  13. Article
  14. Review
  15. The Role of Nonerythroid SpectrinJournal of oncology · 2019
    Review
  16. Article
  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

9 authors at 2 institutions in 2 countries.

Peter M BenzInstitute of Clinical Biochemistry and Pathobiochemistry, University of Würzburg, D-97080 Würzburg, Germany.
Constanze Blume
Jan Moebius
Chris Oschatz
Kai Schuh
Albert Sickmann
Ulrich Walter
Stephan M Feller
Thomas Renné
University of Würzburg · DEJohn Radcliffe Hospital · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Directed cortical actin assembly is the driving force for intercellular adhesion. Regulated by phosphorylation, vasodilator-stimulated phosphoprotein (VASP) participates in actin fiber formation. We screened for endothelial proteins, which bind to VASP, dependent on its phosphorylation status. Differential proteomics identified alphaII-spectrin as such a VASP-interacting protein. alphaII-Spectrin binds to the VASP triple GP(5)-motif via its SH3 domain. cAMP-dependent protein kinase-mediated VASP phosphorylation at Ser157 inhibits alphaII-spectrin-VASP binding. VASP is dephosphorylated upon formation of cell-cell contacts and in confluent, but not in sparse cells, alphaII-spectrin colocalizes with nonphosphorylated VASP at cell-cell junctions. Ectopic expression of the alphaII-spectrin SH3 domain at cell-cell contacts translocates VASP, initiates cortical actin cytoskeleton formation, stabilizes cell-cell contacts, and decreases endothelial permeability. Conversely, the permeability of VASP-deficient endothelial cells (ECs) and microvessels of VASP-null mice increases. Reconstitution of VASP-deficient ECs rescues barrier function, whereas alphaII-spectrin binding-deficient VASP mutants fail to restore elevated permeability. We propose that alphaII-spectrin-VASP complexes regulate cortical actin cytoskeleton assembly with implications for vascular permeability.

Indexed as

Actin CytoskeletonAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCell AdhesionCell Adhesion MoleculesEndothelial CellsIntercellular JunctionsMiceMicrofilament ProteinsMolecular Sequence DataPhosphoproteinsPhosphorylationProtein Interaction Domains and MotifsProtein Interaction MappingCarrier ProteinsCell Adhesion MoleculesMicrofilament ProteinsPhosphoproteinsSpectrinVasodilator-Stimulated Phosphoprotein

Identifiers

PMID18195108
PMCPMC2213610
OpenAlexW2020179019

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.