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3-Phosphoglycerate-dependent protein phosphorylation.

T Ueda, D G Plagens

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1987
    PubMed
    Summary
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    A novel protein kinase activity, dependent on the glycolytic intermediate 3-phosphoglycerate, has been identified in mammalian tissues. This enzyme specifically phosphorylates proteins, particularly in the brain, suggesting a new regulatory pathway.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cellular Signaling

    Background:

    • Protein phosphorylation is crucial for biological regulation.
    • Known protein kinases are often linked to extracellular signals or second messengers.
    • Specific substrates for many kinases have been identified.

    Purpose of the Study:

    • To investigate the role of the glycolytic intermediate 3-phosphoglycerate in protein phosphorylation.
    • To characterize novel protein phosphorylation systems in mammalian tissues.

    Main Methods:

    • Investigated protein phosphorylation in mammalian tissues.
    • Characterized 3-phosphoglycerate-dependent phosphorylation systems.
    • Compared these systems to known kinases (e.g., cAMP, cGMP, Ca2+, calmodulin, protein kinase C, casein kinase II).

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  • Identified protein substrates in brain and non-nervous tissues.

    • Main Results:

    • 3-phosphoglycerate significantly stimulates phosphorylation of specific proteins in mammalian tissues.
    • At least two distinct 3-phosphoglycerate-dependent phosphorylation systems exist in the brain.
    • These systems are insensitive to common activators like cAMP, cGMP, Ca2+, calmodulin, and protein kinase C.
    • Prominent substrates in bovine brain (72 and 155 kDa) are not found in non-nervous tissues.
    • 3-phosphoglycerate affects different proteins in non-nervous tissues.

    Conclusions:

    • Evidence suggests the existence of a previously undescribed protein kinase, termed 3-phosphoglycerate-dependent protein kinase.
    • This novel kinase plays a role in mammalian protein phosphorylation, with distinct characteristics in neural and non-neural tissues.