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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 405-417 
    ISSN: 0886-1544
    Keywords: vinculin ; focal contacts ; microfilaments ; transformation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Talin is a recently identified cytoskeletal protein with a polypeptide molecular weight of 215,000 daltons. In cultured fibroblasts talin has been localized by immunofluorescence in adhesion plaques (focal contacts), in the ruffling membranes and leading lamellae of the cell periphery, and in fibrillar patterns that align with microfilament bundles and/or with cell surface fibronectin. These cellular locations suggest that the protein could function either in the attachment of microfilaments to the plasma membane or in the organization of microfilaments close to membrane attachment sites. Cell transformation by viruses such as Rous sarcoma virus disrupts the normal organization of talin, and in most transformed cells talin appears distributed diffusely through the cytoplasm. In a few cells talin is detected in doughnut-shaped aggregates, as a ring surrounding a central core of actin. The significance of these structures is uncertain, but in some cells the individual structures will condense to form much larger aggregates with a striking appearance when viewed by immunofluoresence microscopy.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 31-36 
    ISSN: 0730-2312
    Keywords: vinculin ; metavinculin ; talin ; platinum shadowing ; self-association ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Vinculin, a 130,000-dalton protein localized to adhesion plaques, and metavinculin, a 150,-000 dalton protein closely related to vinculin, have been studied using rotary shadowing and electron microscopy. Both proteins have globular head regions attached to rod-shaped tail domains. Vinculin and metavinculin also both form complexes consisting of four to six individual molecules. These multimers are formed by head-to-head as well as tail-to-tail interactions.Talin, another protein which has been localized to adhesion plaques and binds to both vinculin and metavinculin, has also been investigated using shadowing techniques. Talin is an elongated, flexible molecule in high ionic strength buffers, as shown here by rotary shadowing and negative stain electron microscopy.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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