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Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
Open accessAbstract
The cystic fibrosis transmembrane conductance regulator (CFTR) plays a central role in transepithelial ion transport by acting as a tightly regulated apical chloride channel. Regulation is achieved by the concerted action of ATP at conserved nucleotide binding folds and serine phosphorylation at multiple sites by protein kinases A (PKA) and C (PKC). A previous investigation concluded that activation by PKA is critically dependent on phosphorylation at four of the nine predicted PKA sites in the R domain (S660A, S737A, S795A, S813A), because a "Quad" mutant lacking these sites could not be activated. We show in the present work that not only can this mutant be phosphorylated and activated, but a mutant in which all 10 predicted PKA sites have been altered still retains significant PKA-activated function. Potentiation of the PKA response by PKC is also preserved in this mutant. Thus CFTR may be regulated by cryptic PKA sites which also mediate interactions between different kinases. Such hierarchical phosphorylation of CFTR by obvious and cryptic PKA sites could provide a metered response to secretagogues.
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Cited by
GENETIC ANALYSIS OF THE MULTIDRUG TRANSPORTER
Gottesman, M. M., Hrycyna, C. A., Schoenlein, P. V., Germann, U. A., & Pastan, I. (1995) · Annual Review of Genetics · doi:10.1146/annurev.ge.29.120195.003135 · Cited by 478
How do protein kinases recognize their substrates?
Pinna, L. A., & Ruzzene, M. (1996) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(96)00083-3 · Cited by 470
Structure of nucleotide‐binding domain 1 of the cystic fibrosis transmembrane conductance regulator
Lewis, H. A., Buchanan, S. G., Burley, S. K., Conners, K., Dickey, M., Dorwart, M., Fowler, R., Gao, X., Guggino, W. B., Hendrickson, W. A., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600040 · Cited by 409
Hwang, T. C., Nagel, G., Nairn, A. C., & Gadsby, D. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4698 · Cited by 263
Structure, Gating, and Regulation of the CFTR Anion Channel
Csanády, L., Vergani, P., & Gadsby, D. C. (2019) · Physiological Reviews · doi:10.1152/physrev.00007.2018 · Cited by 262
Metadata
- Authors
- Chang, X. B., Tabcharani, J. A., Hou, Y. X., Jensen, T. J., Kartner, N., Alon, N., Hanrahan, J. W., & Riordan, J. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-05
- Volume
- 268
- Issue
- 15
- Pages
- 11304-11311
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1638694981
- Cited by
- 296
- References
- 0
- FWCI
- 24.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. https://app.cochat.ai/papers/10.1016/s0021-9258(18)82125-1
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- Chang, X. B., Tabcharani, J. A., Hou, Y. X., Jensen, T. J., Kartner, N., Alon, N., Hanrahan, J. W., & Riordan, J. R. (1993). Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)82125-1
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