ADP-Ribosylation of the Neuronal Phosphoprotein B-50/GAP-43 |
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Authors: | Philip J. Coggins Kim McLean y Nagy Henk Zwiers |
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Affiliation: | Departments of Medical Physiology and Medical Biochemistry, University of Calgary, Health Sciences Centre, Calgary, Alberta, Canada |
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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. |
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Keywords: | ADP-ribosylation Calmodulin B-50/GAP-43 Neuronal proteins Phosphoproteins Protein kinase C |
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