The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 channels by phosphorylation and ATP hydrolysis.
Open accessAbstract
Opening of cystic fibrosis transmembrane conductance regulator (CFTR) Cl channels requires their phosphorylation by protein kinase A followed by exposure to ATP. We examined the interaction between nucleotides and phosphorylated CFTR channels by recording currents in intact cardiac myocytes and in excised patches. We found that, although the hydrolysis-resistant ATP analogue 5'-adenosine(beta,gamma- imino)triphosphate (AMP-PNP) cannot open phosphorylated CFTR channels, it can cause channels opened by ATP to remain open for many minutes. This suggests that ATP action at one site on CFTR is a prerequisite for AMP-PNP action at a second site. However, this action of AMP-PNP is restricted to highly phosphorylated CFTR channels, which, in the presence of ATP, display a relatively high open probability, but is not seen in partially phosphorylated CFTR channels, which have a low open probability in the presence of ATP. Our findings argue that incremental phosphorylation differentially regulates the interactions between nucleotides and the two nucleotide binding domains of CFTR. The nature of those interactions suggests that ATP hydrolysis at one nucleotide binding domain controls channel opening and ATP hydrolysis at the other regulates channel closing.
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Cites
Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNA
Riordan, J. R., Rommens, J. M., Kerem, B.-S., Alon, N., Rozmahel, R., Grzelczak, Z., Zielenski, J., Lok, S., Plavsic, N., Chou, J.-L., et al. (1989) · Science · doi:10.1126/science.2475911 · Cited by 7,418
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Okadaic acid: a new probe for the study of cellular regulation
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Calcium tolerant ventricular myocytes prepared by preincubation in a ?KB medium?
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Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
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Characterization of microcystin-LR, a potent inhibitor of type 1 and type 2A protein phosphatases.
Honkanen, R. E., Zwiller, J., Moore, R. E., Daily, S. L., Khatra, B. S., Dukelow, M., & Boynton, A. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45384-1 · Cited by 588
Nucleoside triphosphates are required to open the CFTR chloride channel
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Mode of regulation of the ACh-sensitive K-channel by the muscarinic receptor in rabbit atrial cells
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Phosphorylation of the cystic fibrosis transmembrane conductance regulator.
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Cited by
Thomas, P. M., Cote, G. J., Wohllk, N., Haddad, B., Mathew, P. M., Rabl, W., Aguilar-Bryan, L., Gagel, R. F., & Bryan, J. (1995) · Science · doi:10.1126/science.7716548 · Cited by 806
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
Self-citationMgATP activates the β cell K ATP channel by interaction with its SUR1 subunit
Gribble, F. M., Tucker, S. J., Haug, T., & Ashcroft, F. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.7185 · Cited by 171
Metadata
- Authors
- Hwang, T. C., Nagel, G., Nairn, A. C., & Gadsby, D. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-05-24
- Volume
- 91
- Issue
- 11
- Pages
- 4698-4702
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2082244393
- Cited by
- 263
- References
- 23
- FWCI
- 25.90
- Type
- journal article
- Language
- en
- Open access
- green
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- Hwang, T. C., Nagel, G., Nairn, A. C., & Gadsby, D. C. (1994). Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 channels by phosphorylation and ATP hydrolysis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.11.4698
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
