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ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase.
Open accessAbstract
In the presence of ATP and a cytosolic factor, cholera toxin fragment A1 catalyzes the transfer of ADP-ribose from NAD to a number of soluble and membrane-bound proteins of the pigeon erythrocyte. Evidence is presented that suggests that the most readily modified membrane protein (Mr 42,000) is the adenylate cyclase-associated GTP-binding protein. Its modification by toxin is stimulated by guanine nucleotides. Adenylate cyclase activity increases in parallel with the addition of ADP-ribose to this protein and decreases in parallel with the subsequent reversal of ADP-ribosylation by toxin and nicotinamide. The protein is only accessible to toxin A subunits if the erythrocytes are lysed. When adenylate cyclase activity reaches a maximum, the number of ADP-ribose residues bound to this protein (about 1500 per cell) is similar to the reported number of beta-adrenergic receptors.
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Citations
Cited by
Forskolin: unique diterpene activator of adenylate cyclase in membranes and in intact cells.
Seamon, K. B., Padgett, W., & Daly, J. W. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3363 · Cited by 1,658
Bacterial toxins: cellular mechanisms of action
Middlebrook, J. L., & Dorland, R. B. (1984) · Microbiological Reviews · doi:10.1128/mmbr.48.3.199-221.1984 · Cited by 357
Role of Vibrio cholerae neuraminidase in the function of cholera toxin
Galen, J. E., Ketley, J. M., Fasano, A., Richardson, S. H., Wasserman, S. S., & Kaper, J. B. (1992) · Infection and Immunity · doi:10.1128/iai.60.2.406-415.1992 · Cited by 177
Campbell, K. M., de Lecea, L., Severynse, D. M., Caron, M. G., McGrath, M. J., Sparber, S. B., Sun, L.-Y., & Burton, F. H. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-12-05044.1999 · Cited by 170
Hews, C. L., Cho, T., Rowley, G., & Raivio, T. L. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00313 · Cited by 168
Metadata
- Authors
- Gill, D. M., & Meren, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1978-07
- Volume
- 75
- Issue
- 7
- Pages
- 3050-3054
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2120640452
- Cited by
- 735
- References
- 0
- FWCI
- 23.47
- Type
- journal article
- Language
- en
- Open access
- green
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- Gill, D. M., & Meren, R. (1978). ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.75.7.3050
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