Abstract
THERE is considerable interest in phosphoprotein metabolism in the brain and the effects of neurotransmitters on the turnover of phosphate in membrane proteins1. Emphasis has been placed on the phosphorylation of proteins of synaptosomal membranes, but in addition myelin comprises a considerable proportion of the total substrate activity for a soluble protein kinase of brain2. In the following paper Miyamoto et al.3 show that this kinase, which is stimulated by adenosine 3′, 5′-cycle monophosphate (cyclic AMP), phosphorylates the basic protein of myelin. Besides being a substrate for this soluble kinase the basic protein was found to be phosphorylated by an endogenous kinase of myelin3. Carnegie et al.4 demonstrated that a protein kinase from rabbit muscle would selectively phosphorylate certain serine and threonine residues in the basic proteins of rat and human myelin. Soluble protein kinases from brain and muscle seem to phosphorylate similar sites in histones5. We present evidence here that the endogenous protein kinase of myelin phosphorylates the basic protein, but not the proteolipid protein, and that the site of phosphorylation by this endogenous kinase is quite different from the site phosphorylated by soluble protein kinase.
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CARNEGIE, P., DUNKLEY, P., KEMP, B. et al. Phosphorylation of selected serine and threonine residues in myelin basic protein by endogenous and exogenous protein kinases. Nature 249, 147–150 (1974). https://doi.org/10.1038/249147a0
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DOI: https://doi.org/10.1038/249147a0
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