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The cytoskeletal protein vinculin is acylated by myristic acid

S Kellie, N M Wigglesworth

    FEBS Letters
    |March 23, 1987
    PubMed

    Insights

    Vinculin, a protein in cell adhesion plaques, is modified by myristic acid acylation. This modification occurs in various cellular locations and is present in Rous sarcoma virus-transformed cells.

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • The interaction between microfilament bundles and the plasma membrane in non-muscle cells is not fully understood.
    • Vinculin, a 130 kDa protein, is found in adhesion plaques and is hypothesized to anchor microfilaments to the membrane.

    Purpose of the Study:

    • To investigate the biochemistry of vinculin in more detail.
    • To determine the role of vinculin modification in its subcellular localization and function.

    Main Methods:

    • Biochemical analysis of vinculin from chick embryo fibroblasts.
    • Investigation of protein acylation, specifically myristic acid modification.

    Main Results:

    • A fraction of vinculin in chick embryo fibroblasts undergoes acylation by myristic acid.
    • Myristic acid modification was detected in membrane-bound, cytoskeletal, and cytosolic vinculin.
    • Acylated vinculin was also found in cells transformed by Rous sarcoma virus.

    Conclusions:

    • Myristic acid acylation of vinculin does not dictate its preferential subcellular localization.
    • The presence of myristic acid in vinculin from Rous sarcoma virus-transformed cells suggests a potential role in viral transformation or cell adhesion dynamics.

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