Vinculin
- PMID: 2112986
- DOI: 10.1002/cm.970160102
Vinculin
Abstract
Vinculin is clearly a key element in the transmembrane assemblages that link cells to each other or to the substrate. However, despite all the studies that have been done on the protein, we still do not know its function within these assemblages. The bulk of the biochemical and cell biological evidence suggests that, in some unknown way, its presence in the junctions may be involved in the stable association of actin with the membrane, yet vinculin by itself does not appear to interact with actin. In the future, identification of additional junctional molecules that interconnect actin and vinculin may resolve this dilemma. Alternatively, studies with vinculin that is phosphorylated or acylated may yield clues to its function. Perhaps the complexity of the protein composition of microfilament-containing junctions suggests that protein assemblages rather than individual proteins provide novel functions. As new proteins belonging to these junctions are discovered, it will be important to assess their interaction with already known components such as vinculin and to ask if the protein combination has a particular function.
Similar articles
-
Vinculin and alpha-catenin: shared and unique functions in adherens junctions.Bioessays. 1998 Sep;20(9):733-40. doi: 10.1002/(SICI)1521-1878(199809)20:9<733::AID-BIES6>3.0.CO;2-H. Bioessays. 1998. PMID: 9819562 Review.
-
Vinculin, VASP, and profilin are coordinately regulated during actin remodeling in epithelial cells, which requires de novo protein synthesis and protein kinase signal transduction pathways.J Cell Physiol. 2004 Aug;200(2):277-90. doi: 10.1002/jcp.20009. J Cell Physiol. 2004. PMID: 15174098
-
Actin-associated proteins in human neutrophils: identification and reorganization upon cell activation.Eur J Cell Biol. 1989 Aug;49(2):366-72. Eur J Cell Biol. 1989. PMID: 2506050
-
Vinculin promotes cell spreading by mechanically coupling integrins to the cytoskeleton.Exp Cell Res. 1997 Feb 25;231(1):14-26. doi: 10.1006/excr.1996.3451. Exp Cell Res. 1997. PMID: 9056408
-
[The interactions of actin cell and membrane skeleton proteins with lipids].Postepy Biochem. 2009;55(2):207-22. Postepy Biochem. 2009. PMID: 19824478 Review. Polish.
Cited by
-
Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton.J Cell Biol. 1992 Dec;119(6):1573-87. doi: 10.1083/jcb.119.6.1573. J Cell Biol. 1992. PMID: 1469049 Free PMC article.
-
The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-alpha catenin fusion molecules.J Cell Biol. 1994 Oct;127(1):235-45. doi: 10.1083/jcb.127.1.235. J Cell Biol. 1994. PMID: 7929566 Free PMC article.
-
Functional domains of alpha-catenin required for the strong state of cadherin-based cell adhesion.J Cell Biol. 1999 Mar 22;144(6):1311-22. doi: 10.1083/jcb.144.6.1311. J Cell Biol. 1999. PMID: 10087272 Free PMC article.
-
Calreticulin modulates cell adhesiveness via regulation of vinculin expression.J Cell Biol. 1996 Dec;135(6 Pt 2):1913-23. doi: 10.1083/jcb.135.6.1913. J Cell Biol. 1996. PMID: 8991101 Free PMC article.
-
Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin.J Cell Biol. 1994 Sep;126(5):1231-40. doi: 10.1083/jcb.126.5.1231. J Cell Biol. 1994. PMID: 8063860 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials