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Lipid modifications of G proteins: alpha subunits are palmitoylated.
Open accessAbstract
A small number of membrane-associated proteins are reversibly and covalently modified with palmitic acid. Palmitoylation of G-protein alpha and beta subunits was assessed by metabolic labeling of subunits expressed in simian COS cells or insect Sf9 cells. The fatty acid was incorporated into all of the alpha subunits examined (alpha s, alpha o, alpha i1, alpha i2, alpha i3, alpha z, and alpha q), including those that are also myristoylated (alpha o, alpha i, and alpha z). Palmitate was released by treatment with base, suggesting attachment to the protein through a thioester or ester bond. Limited tryptic digestion of activated alpha o and alpha s resulted in release of the amino-terminal portions of the proteins and radioactive palmitate. These data are consistent with palmitoylation of the proteins near their amino termini, most likely on Cys-3. Reversible acylation of G-protein alpha subunits may provide an additional mechanism for regulation of signal transduction.
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Cited by
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Melkonian, K. A., Ostermeyer, A. G., Chen, J. Z., Roth, M. G., & Brown, D. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3910 · Cited by 629
Human RAS Superfamily Proteins and Related GTPases
Colicelli, J. (2004) · Science's STKE · doi:10.1126/stke.2502004re13 · Cited by 582
Weinstein, L. S., Yu, S., Warner, D. R., & Liu, J. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.5.0439 · Cited by 420
Isoforms of Mammalian Adenylyl Cyclase: Multiplicities of Signaling
Sunahara, R. K. (2002) · Molecular Interventions · doi:10.1124/mi.2.3.168 · Cited by 406
Shenoy-Scaria, A. M., Dietzen, D. J., Kwong, J., Link, D. C., & Lublin, D. M. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.2.353 · Cited by 391
Metadata
- Authors
- Linder, M. E., Middleton, P., Hepler, J. R., Taussig, R., Gilman, A. G., & Mumby, S. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-04-15
- Volume
- 90
- Issue
- 8
- Pages
- 3675-3679
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1978686382
- Cited by
- 348
- References
- 0
- FWCI
- 11.62
- Type
- journal article
- Language
- en
- Open access
- green
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- Linder, M. E., Middleton, P., Hepler, J. R., Taussig, R., Gilman, A. G., & Mumby, S. M. (1993). Lipid modifications of G proteins: alpha subunits are palmitoylated. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.8.3675
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