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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Phosphorylation of the "37000 component" of the troponin complex (troponin-t)

S V Perry, H A Cole

    The Biochemical Journal
    |February 1, 1973
    PubMed

    Insights

    Phosphorylation by phosphorylase b kinase primarily targets the 37000 component of the troponin complex. This phosphorylation occurs with [gamma-(32)P]ATP, affecting the inhibitory protein but not the calcium-binding protein.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Muscle Physiology

    Background:

    • The troponin complex is crucial for muscle contraction regulation.
    • Phosphorylation plays a key role in modulating protein function.
    • Understanding troponin phosphorylation is vital for muscle physiology research.

    Purpose of the Study:

    • To investigate the specific sites and components of the troponin complex phosphorylated by phosphorylase b kinase.
    • To determine the role of different troponin subunits in the phosphorylation process.

    Main Methods:

    • Incubation of the troponin complex with phosphorylase b kinase and [gamma-(32)P]ATP.
    • Analysis of phosphorus association with different troponin components.
    • Quantification of phosphorylated subunits.

    Main Results:

    • The troponin complex contains approximately 1 mol of phosphorus per 80000g.
    • The 37000 component is significantly phosphorylated (0.6 mol of P/mol).
    • Phosphorylase b kinase specifically phosphorylates the inhibitory protein and the 37000 component, sparing the calcium-binding protein.

    Conclusions:

    • The 37000 component of the troponin complex is a primary target for phosphorylation by phosphorylase b kinase.
    • Phosphorylation of the troponin complex by phosphorylase b kinase involves specific subunits, highlighting regulatory mechanisms in muscle function.

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