ADP-Ribosylation of Membrane Proteins in Cholinergic Nerve Terminals
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 M_r = 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 M_r = 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.
Additional Information
© 1982 International Society for Neurochemistry. Received July 13, 1981; accepted October 22, 1981. We thank Z. Zimmer for technical assistance and A. Levitzki for advice and support. This research was supported by the United States National Institutes of Health (grant GM-26604 to A. L., and Research Career Development Awards NS-272 to H.A.L. and NS-160 to M.L.S.) and by grants from the Muscular Dystrophy Association of America to Tel Aviv University and to the California Institute of Technology.Additional details
- Eprint ID
- 106001
- Resolver ID
- CaltechAUTHORS:20201012-160322257
- GM-26604
- NIH
- NS-272
- NIH Postdoctoral Fellowship
- NS-160
- NIH Postdoctoral Fellowship
- Muscular Dystrophy Association of America
- Created
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2020-10-13Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field