ArticleThe Journal of cell biology1986
Vinculin interaction with permeabilized cells: disruption and reconstitution of a binding site.
Article in The Journal of cell biology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Force transduction by Triton cytoskeletons.The Journal of cell biology · 2002Article
- A cell-free system to study regulation of focal adhesions and of the connected actin cytoskeleton.Molecular biology of the cell · 1999Article
- Isolation and contraction of the stress fiber.Molecular biology of the cell · 1998Article
- Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex.Molecular biology of the cell · 1995Article
- Tyrosine phosphorylation and cytoskeletal tension regulate the release of fibroblast adhesions.The Journal of cell biology · 1995Article
- Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin.The Journal of cell biology · 1994Article
- Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA.The Journal of cell biology · 1992Article
- Accumulation of talin in nodes at the edge of the lamellipodium and separate incorporation into adhesion plaques at focal contacts in fibroblasts.The Journal of cell biology · 1991Article
- The structure and function of alpha-actinin.Journal of muscle research and cell motility · 1989Review
- Identification of two distinct functional domains on vinculin involved in its association with focal contacts.The Journal of cell biology · 1989Article
- Interaction of the cytoskeleton with the plasma membrane.The Journal of membrane biology · 1987Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fluorescently labeled vinculin binds to focal contact areas in permeabilized cells independent of actin (Avnur, Z., J. V. Small, and B. Geiger, 1983, J. Cell Biol., 96:1622-1630), but the nature of the binding site is unknown. In this study we have examined the interaction of vinculin with these sites in permeabilized L6 myoblasts to define conditions that perturb the binding and subsequently to reconstitute it. Mild treatment with low concentrations of protease prevents vinculin incorporation without gross changes in the cytoskeleton or extensive protein breakdown. Exposure to buffers of moderate ionic strength also reduces subsequent vinculin binding without large morphological effects. These extraction conditions were used to obtain a fraction from gizzard which was able to restore the vinculin localization. Talin, actin, and vinculin itself were able to alter the binding of labeled vinculin to permeabilized cells and each also interacted with vinculin in gel overlays; however, they were unable to reconstitute the binding site in treated permeabilized cells. The results show a requirement for an as yet unidentified protein to capacitate vinculin binding to focal contact sites and suggest that this protein is peripheral and interacts directly with the binding site.
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