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ADP-Ribosylation of the Neuronal Phosphoprotein B-50/GAP-43
Authors:Philip J. Coggins  Kim McLean  y Nagy  Henk Zwiers
Affiliation:Departments of Medical Physiology and Medical Biochemistry, University of Calgary, Health Sciences Centre, Calgary, Alberta, Canada
Abstract:Abstract: The neuronal phosphoprotein B-50/GAP-43 is associated with growth and regeneration within the nervous system and its posttranslational status can be correlated with its cellular localization during growth and regeneration. Recently, B-50 has been shown to interact with certain G protein subunits. Regulation of G protein-mediated signal transduction may involve ADP-ribosylation in vivo. In the present study we have demonstrated that B-50 is a substrate for endogenous ADP-ribosyltransferases. The results are discussed with respect to the possible interaction of B-50 with G proteins, but also with regard to the posttranslational modification of B-50 by all major regulatory mechanisms that act at, or through, the neuronal membrane.
Keywords:ADP-ribosylation    Calmodulin    B-50/GAP-43    Neuronal proteins    Phosphoproteins    Protein kinase C
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