The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structural Determinants of Pip2 Regulation of Inward Rectifier KATP Channels
Open accessAbstract
Phosphatidylinositol 4,5-bisphosphate (PIP2) activates KATP and other inward rectifier (Kir) channels. To determine residues important for PIP2 regulation, we have systematically mutated each positive charge in the COOH terminus of Kir6.2 to alanine. The effects of these mutations on channel function were examined using 86Rb efflux assays on intact cells and inside-out patch-clamp methods. Both methods identify essentially the same basic residues in two narrow regions (176–222 and 301–314) in the COOH terminus that are important for the maintenance of channel function and interaction with PIP2. Only one residue (R201A) simultaneously affected ATP and PIP2 sensitivity, which is consistent with the notion that these ligands, while functionally competitive, are unlikely to bind to identical sites. Strikingly, none of 13 basic residues in the terminal portion (residues 315–390) of the COOH terminus affected channel function when neutralized. The data help to define the structural requirements for PIP2 sensitivity of KATP channels. Moreover, the regions and residues defined in this study parallel those uncovered in recent studies of PIP2 sensitivity in other inward rectifier channels, indicating a common structural basis for PIP2 regulation.
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Cites
Association and Stoichiometry of KATP Channel Subunits
Clement, J. P., Kunjilwar, K., Gonzalez, G., Schwanstecher, M., Panten, U., Aguilar-Bryan, L., & Bryan, J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80321-9 · Cited by 692
Membrane Phospholipid Control of Nucleotide Sensitivity of K ATP Channels
Shyng, S.-L., & Nichols, C. G. (1998) · Science · doi:10.1126/science.282.5391.1138 · Cited by 559
Self-citationMolecular Analysis of ATP-sensitive K Channel Gating and Implications for Channel Inhibition by ATP
Trapp, S., Proks, P., Tucker, S. J., & Ashcroft, F. M. (1998) · The Journal of General Physiology · doi:10.1085/jgp.112.3.333 · Cited by 170 · cited 1×
“2 channels is labile; point mutations can render the channel very ATP-insensitive (Tucker et al., 1997, 1998; Drain et al., 1998; Trapp et al., 1998; Enkvetchakul et al., 2000; Loussouarn et al., 2000), and any mutation, or manipulation, that increases open state stability reduces the apparent ATP…”
Background
Cited by
Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles
Hibino, H., Inanobe, A., Furutani, K., Murakami, S., Findlay, I., & Kurachi, Y. (2010) · Physiological Reviews · doi:10.1152/physrev.00021.2009 · Cited by 1,539
Gloyn, A. L., Pearson, E. R., Antcliff, J. F., Proks, P., Bruining, G. J., Slingerland, A. S., Howard, N., Srinivasan, S., Silva, J. M. C. L., Molnes, J., et al. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa032922 · Cited by 1,137
KATP channels as molecular sensors of cellular metabolism
Nichols, C. G. (2006) · Nature · doi:10.1038/nature04711 · Cited by 851
Self-citationHyperinsulinism in Infancy: From Basic Science to Clinical Disease
DUNNE, M. J., COSGROVE, K. E., SHEPHERD, R. M., AYNSLEY-GREEN, A., & LINDLEY, K. J. (2004) · Physiological Reviews · doi:10.1152/physrev.00022.2003 · Cited by 294
Electrophysiology of Islet Cells
Drews, G., Krippeit-Drews, P., & Düfer, M. (2010) · Advances in Experimental Medicine and Biology · doi:10.1007/978-90-481-3271-3_7 · Cited by 152
Metadata
- Authors
- Shyng, S.-L., Cukras, C. A., Harwood, J., & Nichols, C. G.
- Venue
- The Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 2000-10-16
- Volume
- 116
- Issue
- 5
- Pages
- 599-608
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- OpenAlex
- W1991675939
- Cited by
- 202
- References
- 3
- FWCI
- 4.39
- Type
- journal article
- Language
- en
- Open access
- green
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- Shyng, S.-L., Cukras, C. A., Harwood, J., & Nichols, C. G. (2000). Structural Determinants of Pip2 Regulation of Inward Rectifier KATP Channels. The Journal of General Physiology. https://doi.org/10.1085/jgp.116.5.599
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