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Phosphate groups modifying myelin basic proteins are metabolically labile; methyl groups are stable.

K C DesJardins, P Morell

    The Journal of Cell Biology
    |August 1, 1983
    PubMed
    Summary
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    Myelin basic protein phosphate groups rapidly turnover within minutes, unlike their peptide backbone and methyl groups which have half-lives of months. This suggests myelin proteins are more dynamic than previously thought.

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Cell Biology

    Background:

    • Myelin basic protein (MBP) is a major component of myelin.
    • The metabolic stability of MBP has been poorly understood.
    • Previous studies suggested a static role for myelin proteins.

    Purpose of the Study:

    • To investigate the turnover rate of phosphate groups in myelin basic protein.
    • To compare the metabolic stability of MBP's phosphate groups with its peptide backbone and methyl modifications.
    • To understand the dynamic nature of myelin proteins in vivo.

    Main Methods:

    • Rats received intracranial injections of radioactive phosphate ([33P]orthophosphoric acid) and methionine ([methyl-3H]methionine).
    • Radioactivity in isolated myelin and its subfractions was measured over one month.

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  • Turnover rates were calculated based on incorporation and decay kinetics.

    • Main Results:

    • Myelin basic protein phosphate groups exhibited rapid turnover, with most turning over in minutes.
    • The peptide backbone and methyl groups of MBP had metabolic half-lives of months.
    • Phosphate group turnover was independent of myelin synthesis rate but proportional to myelin amount.

    Conclusions:

    • Myelin basic protein phosphate groups undergo rapid metabolic exchange, challenging the notion of static myelin.
    • These findings suggest that MBP is accessible to the cytoplasm in vivo.
    • The distinct turnover rates highlight differential regulation of protein modifications in myelin.