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  • Title: ADP-ribosylation of membrane proteins in cholinergic nerve terminals.
    Author: Lester HA, Steer ML, Michaelson DM.
    Journal: J Neurochem; 1982 Apr; 38(4):1080-6. PubMed ID: 7062032.
    Abstract:
    Lysed Torpedo synaptosomes or washed synaptosomal membranes were incubated with [32P]NAD+ and subjected to electrophoresis on SDS-polyacrylamide gels. More than eight membrane proteins were ADP-ribosylated. The most intensely labeled proteins were those of Mr = 62,000 and 82,000. Radiolabeling was more intense in synaptosomes than in other subcellular fractions. Cholera toxin caused ribosylation of additional synaptosomal proteins with Mr = 42,000 and (in some preparations) 49,000. Neither endogenous nor cholera toxin-catalyzed ADP-ribosylation required added guanyl nucleotides. Cholera toxin increased the adenylate cyclase activity of synaptosomal membranes, suggesting that the cholera toxin substrates are regulatory components of adenylate cyclase in these synaptosomes.
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