Evidence map›Paper›PMID 8615776›Full record

ArticleThe Biochemical journal1996

Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites.

J Weekes, S T Barry, D R Critchley

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 149 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Vinculin in cell-cell and cell-matrix adhesions.Cellular and molecular life sciences : CMLS · 2017
    Review
  6. Article
  7. A Structural Model for Vinculin Insertion into PIPStructure (London, England : 1993) · 2017
    Article
  8. Article
  9. Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Dimer asymmetry defines α-catenin interactions.Nature structural & molecular biology · 2013
    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 1 institution in 1 country.

J WeekesDepartment of Biochemistry, University of Leicester, U.K.
S T Barry
D R Critchley
University of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chick vinculin polypeptides expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins have been used to identify the sites involved in the intramolecular association between the 90 kDa N-terminal head and the 30 kDa C-terminal tail region of the vinculin molecule. Fusion proteins spanning vinculin residues 1-258 and 1-398, immobilized on glutathione-agarose beads, were shown to bind a C-terminal vinculin polypeptide spanning residues 881-1066 (liberated from GST by thrombin cleavage). However, the C-terminal polypeptide did not bind to a fusion protein spanning residues 399-881 or to itself. Binding was dependent on residues 167-207 within the N-terminal polypeptide, a sequence also essential for talin binding. Conversely, the 90 kDa head polypeptide was shown to bind to residues 1029-1036 in the tail region of vinculin. The association of the head and tail was inhibited by acidic, but not neutral, phospholipids. Pre-incubation of vinculin with acidic phospholipids exposed the binding site for F-actin and a phosphorylation site for protein kinase C. The phosphorylation site was located in the tail region of the vinculin molecule. These results raise the possibility that acidic phospholipids play a role in regulating the activity of vinculin and therefore the assembly of both cell-cell and cell-matrix adherens-type junctions.

Indexed as

ActinsAnimalsBinding SitesChickensCloning, MolecularCytoskeletal ProteinsEscherichia coliGlutathione TransferaseIsoenzymesKineticsPaxillinPeptide FragmentsPhospholipidsPhosphoproteinsPhosphorylationProtein Kinase CActinsCytoskeletal ProteinsGlutathione TransferaseIsoenzymesPaxillinPeptide FragmentsPhospholipidsPhosphoproteinsProtein Kinase CPxn protein, ratRecombinant Fusion ProteinsVinculin

Identifiers

PMID8615776
PMCPMC1217131
OpenAlexW2231186867

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.