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Feedback regulation of phospholipase C-beta by protein kinase C.
Open accessAbstract
Treatment of a variety of cells and tissues with 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C (PKC) results in the inhibition of receptor-coupled inositol phospholipid-specific phospholipase C (PLC) activity. To determine whether or not the targets of TPA-activated PKC include one or more isozymes of PLC, studies were carried out with PC12, C6Bu1, and NIH 3T3 cells, which contain at least three PLC isozymes, PLC-beta, PLC-gamma, and PLC-delta. Treatment of the cells with TPA stimulated the phosphorylation of serine residues in PLC-beta, but the phosphorylation state of PLC-gamma and PLC-delta was not changed significantly. Phosphorylation of bovine brain PLC-beta by PKC in vitro resulted in a stoichiometric incorporation of phosphate at serine 887, without any concomitant effect on PLC-beta activity. We propose, therefore, that rather than having a direct effect on enzyme activity, the phosphorylation of PLC-beta by PKC may alter its interaction with a putative guanine nucleotide-binding regulatory protein and thereby prevent its activation.
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Cited by
Kadamur, G., & Ross, E. M. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183750 · Cited by 529
Metadata
- Authors
- Ryu, S. H., Kim, U. H., Wahl, M. I., Brown, A. B., Carpenter, G., Huang, K. P., & Rhee, S. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-10
- Volume
- 265
- Issue
- 29
- Pages
- 17941-17945
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1585941903
- Cited by
- 213
- References
- 0
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Ryu, S. H., Kim, U. H., Wahl, M. I., Brown, A. B., Carpenter, G., Huang, K. P., & Rhee, S. G. (1990). Feedback regulation of phospholipase C-beta by protein kinase C. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)38254-1
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