The vinculin C-terminal hairpin mediates F-actin bundle formation, focal adhesion, and cell mechanical properties
(2011) In Journal of Biological Chemistry 286(52). p.15-45103- Abstract
Vinculin is an essential and highly conserved cell adhesion protein, found at both focal adhesions and adherens junctions, where it couples integrins or cadherins to the actin cytoskeleton. Vinculin is involved in controlling cell shape, motility, and cell survival, and has more recently been shown to play a role in force transduction. The tail domain of vinculin (Vt) contains determinants necessary for binding and bundling of actin filaments. Actin binding to Vt has been proposed to induce formation of a Vt dimer that is necessary for cross-linking actin filaments. Results from this study provide additional support for actin-induced Vt self-association. Moreover, the actin-induced Vt dimer appears distinct from the dimer formed in the... (More)
Vinculin is an essential and highly conserved cell adhesion protein, found at both focal adhesions and adherens junctions, where it couples integrins or cadherins to the actin cytoskeleton. Vinculin is involved in controlling cell shape, motility, and cell survival, and has more recently been shown to play a role in force transduction. The tail domain of vinculin (Vt) contains determinants necessary for binding and bundling of actin filaments. Actin binding to Vt has been proposed to induce formation of a Vt dimer that is necessary for cross-linking actin filaments. Results from this study provide additional support for actin-induced Vt self-association. Moreover, the actin-induced Vt dimer appears distinct from the dimer formed in the absence of actin. To better characterize the role of the Vt strap and carboxyl terminus (CT) in actin binding, Vt self-association, and actin bundling, we employed smaller amino-terminal (NT) and CT deletions that do not perturb the structural integrity of Vt. Although both NT and CT deletions retain actin binding, removal of the CT hairpin (1061-1066) selectively impairs actin bundling in vitro. Moreover, expression of vinculin lacking the CT hairpin in vinculin knock-out murine embryonic fibroblasts affects the number of focal adhesions formed, cell spreading as well as cellular stiffening in response to mechanical force.
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- author
- Shen, Kai ; Tolbert, Caitlin E ; Guilluy, Christophe ; Swaminathan, Vinay S LU ; Berginski, Matthew E ; Burridge, Keith ; Superfine, Richard and Campbell, Sharon L
- publishing date
- 2011-12-30
- type
- Contribution to journal
- publication status
- published
- keywords
- Actins/genetics, Animals, Avian Proteins/genetics, Cells, Cultured, Chickens, Fibroblasts/cytology, Focal Adhesions/genetics, Mice, Mice, Knockout, Protein Binding, Protein Multimerization/physiology, Protein Structure, Tertiary, Vinculin/genetics
- in
- Journal of Biological Chemistry
- volume
- 286
- issue
- 52
- pages
- 15 - 45103
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:22052910
- scopus:84455192508
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M111.244293
- language
- English
- LU publication?
- no
- id
- 3921be26-31f0-4e43-b6d1-6776a15c1f43
- date added to LUP
- 2018-09-07 16:53:39
- date last changed
- 2024-02-14 01:16:01
@article{3921be26-31f0-4e43-b6d1-6776a15c1f43,
abstract = {{<p>Vinculin is an essential and highly conserved cell adhesion protein, found at both focal adhesions and adherens junctions, where it couples integrins or cadherins to the actin cytoskeleton. Vinculin is involved in controlling cell shape, motility, and cell survival, and has more recently been shown to play a role in force transduction. The tail domain of vinculin (Vt) contains determinants necessary for binding and bundling of actin filaments. Actin binding to Vt has been proposed to induce formation of a Vt dimer that is necessary for cross-linking actin filaments. Results from this study provide additional support for actin-induced Vt self-association. Moreover, the actin-induced Vt dimer appears distinct from the dimer formed in the absence of actin. To better characterize the role of the Vt strap and carboxyl terminus (CT) in actin binding, Vt self-association, and actin bundling, we employed smaller amino-terminal (NT) and CT deletions that do not perturb the structural integrity of Vt. Although both NT and CT deletions retain actin binding, removal of the CT hairpin (1061-1066) selectively impairs actin bundling in vitro. Moreover, expression of vinculin lacking the CT hairpin in vinculin knock-out murine embryonic fibroblasts affects the number of focal adhesions formed, cell spreading as well as cellular stiffening in response to mechanical force.</p>}},
author = {{Shen, Kai and Tolbert, Caitlin E and Guilluy, Christophe and Swaminathan, Vinay S and Berginski, Matthew E and Burridge, Keith and Superfine, Richard and Campbell, Sharon L}},
issn = {{1083-351X}},
keywords = {{Actins/genetics; Animals; Avian Proteins/genetics; Cells, Cultured; Chickens; Fibroblasts/cytology; Focal Adhesions/genetics; Mice; Mice, Knockout; Protein Binding; Protein Multimerization/physiology; Protein Structure, Tertiary; Vinculin/genetics}},
language = {{eng}},
month = {{12}},
number = {{52}},
pages = {{15--45103}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{The vinculin C-terminal hairpin mediates F-actin bundle formation, focal adhesion, and cell mechanical properties}},
url = {{http://dx.doi.org/10.1074/jbc.M111.244293}},
doi = {{10.1074/jbc.M111.244293}},
volume = {{286}},
year = {{2011}},
}