Literature DB >> 2112986

Vinculin.

J J Otto1.   

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.

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Year:  1990        PMID: 2112986     DOI: 10.1002/cm.970160102

Source DB:  PubMed          Journal:  Cell Motil Cytoskeleton        ISSN: 0886-1544


  27 in total

1.  Attachment kinetics, proliferation rates and vinculin assembly of bovine osteoblasts cultured on different pre-coated artificial substrates.

Authors:  U Meyer; T Meyer; D B Jones
Journal:  J Mater Sci Mater Med       Date:  1998-06       Impact factor: 3.896

Review 2.  Actin binding proteins--lipid interactions.

Authors:  G Isenberg
Journal:  J Muscle Res Cell Motil       Date:  1991-04       Impact factor: 2.698

3.  Immunofluorescence distribution of actin-associated proteins in human seminiferous tubules of adolescent testes, normal and pathologic.

Authors:  G Santoro; C Romeo; P Impellizzeri; G Cutroneo; A Micali; F Trimarchi; C Gentile
Journal:  J Endocrinol Invest       Date:  2000-06       Impact factor: 4.256

4.  A theoretical analysis for the effect of focal contact formation on cell-substrate attachment strength.

Authors:  M D Ward; D A Hammer
Journal:  Biophys J       Date:  1993-03       Impact factor: 4.033

5.  Focal contact assembly through cytoskeletal polymerization: steady state analysis.

Authors:  M D Ward; D A Hammer
Journal:  J Math Biol       Date:  1994       Impact factor: 2.259

6.  Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis.

Authors:  M Tempel; W H Goldmann; G Isenberg; E Sackmann
Journal:  Biophys J       Date:  1995-07       Impact factor: 4.033

7.  Spatial distribution and functional significance of activated vinculin in living cells.

Authors:  Hui Chen; Daniel M Cohen; Dilshad M Choudhury; Noriyuki Kioka; Susan W Craig
Journal:  J Cell Biol       Date:  2005-05-09       Impact factor: 10.539

8.  Primary mesenchymal cells isolated from SPARC-null mice exhibit altered morphology and rates of proliferation.

Authors:  A D Bradshaw; A Francki; K Motamed; C Howe; E H Sage
Journal:  Mol Biol Cell       Date:  1999-05       Impact factor: 4.138

9.  Fibronectin and laminin in transverse tubules of cardiac myocytes studied by laser confocal microscopy and immunocytochemistry.

Authors:  T Saetersdal; T Larsen; S Rotevatn; H Dalen; P Scheie
Journal:  Histochemistry       Date:  1992-09

10.  Analysis of the suitability of calreticulin inducible HEK cells for adhesion studies: microscopical and biochemical comparisons.

Authors:  Sylvia Papp; Marc P Fadel; Marek Michalak; Michal Opas
Journal:  Mol Cell Biochem       Date:  2007-10-02       Impact factor: 3.396

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