Activation of the atrial KACh channel by the βγ subunits of G proteins or intracellular Na+ ions depends on the presence of phosphatidylinositol phosphates

Proceedings of the National Academy of Sciences of the United States of America

Volumn 95, Issue 3, 1998, Pages 1307-1312

  Sui, Jin Liang ^a,b   Petit Jacques, Jérôme ^a   Logothetis, Diomedes E ^a  

^a CITY UNIVERSITY OF NEW YORK   (United States)

^b CeNeS Pharmaceuticals plc   (United States)

Author keywords

G protein gated K+ channel; Phosphatidylinositol 4,5 bisphosphate

Indexed keywords

ADENOSINE TRIPHOSPHATE; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; INWARDLY RECTIFYING POTASSIUM CHANNEL; MUSCARINIC RECEPTOR; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; POTASSIUM CHANNEL; SODIUM; SODIUM CHANNEL; PROTEIN SUBUNIT;

ANIMAL; ARTICLE; CELL MEMBRANE; CHANNEL GATING; CHICKEN; HEART MUSCLE; METABOLISM; SIGNAL TRANSDUCTION; XENOPUS; ANIMAL CELL; CHICK EMBRYO; CONFERENCE PAPER; EMBRYO; ENZYME ACTIVATION; NONHUMAN; OOCYTE; POTASSIUM TRANSPORT; PRIORITY JOURNAL; PROTEIN ANALYSIS; SODIUM TRANSPORT;

ADENOSINE TRIPHOSPHATE; ANIMALS; CELL MEMBRANE; CHICKENS; G PROTEIN-COUPLED INWARDLY-RECTIFYING POTASSIUM CHANNELS; GTP-BINDING PROTEINS; GUANOSINE TRIPHOSPHATE; ION CHANNEL GATING; MYOCARDIUM; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; RECEPTORS, MUSCARINIC; SIGNAL TRANSDUCTION; SODIUM; SODIUM CHANNELS; XENOPUS;

ANIMALIA;

EID: 0032477641     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.95.3.1307     Document Type: Article

References (38)

1. Sui, J.-L., Chan, K., Langan, M.-N., Vivaudou, M. & Logothetis, D. E. in Advances in Second Messenger and Phosphoprotein Research, eds. Armstrong, D. & Rossie, S., in press.
2. Soejima, M. & Noma, A. (1984) Pflügers Arch. 400, 424-431.
3. Logothetis, D. E., Kurachi, Y., Galper, J., Neer E. J. & Clapham, D. E. (1987) Nature (London) 325, 321-326.
4. Krapivinsky, G., Gordon, E. A., Wickman, K., Velimirovic, B., Krapivinsky, L. & Clapham, D. E. (1995) Nature (London) 374, 135-141.
5. Reuveny, E., Slesinger, P. A., Inglese, J., Morales, J. M., Iniguez-Lluhi, J. A., Lefkowitz, R. J., Bourne, H. R., Jan, Y. N. & Jan, L. Y. (1994) Nature (London) 370, 143-146.
6. Silverman, S. K., Lester, H. A. & Dougherty, D. A. (1996) J. Biol Chem. 271, 30524-30528.
7. Krapivinsky, G., Krapivinsky, L., Wickman, K. & Clapham, D. E. (1995b) J. Biol. Chem. 270, 29059-29062.
8. Kunkel, M. T. & Peralta, E. G. (1995) Cell 83, 443-449.
9. Huang, C.L., Slesinger, P. A., Casey, P. J., Jan, Y. N. & Jan, L. Y. (1995) Neuron 15, 1133-1143.
10. Huang, C.-L., Jan, Y. N. & Jan, L. Y. (1997) FEBS Lett. 405, 291-298.
11. Inanobe, A., Morishige, K. I., Takahashi, N., Ito, H., Yamada, M., Takumi, T., Nishina, H., Takahashi, K., Kanaho, Y., Katada, T. & Kurachi, Y. (1995) Biochem. Biophys. Res. Commun. 212, 1022-1028.
12. Doupnik, C. A., Dessauer, C. W., Slepak, V. Z., Gilman, A. G., Davidson, N. & Lester, H. A. (1996) Neuropharmacology 35, 923-931.
13. Sui, J. L., Chan, K. W. & Logothetis, D. E. (1996) J. Gen. Physiol. 108, 381-391.
14. Hilgemann, D. W. (1997) Annu. Rev. Physiol. 59, 193-220.
15. Hilgemann, D. W. & Ball, R. (1996) Science 273, 956-959.
16. Fan, Z. & Makielski, J. C. (1997) J. Biol. Chem. 272, 5388-5395.
17. Chan, K. W., Langan, M. N., Sui, J. L., Kozak, J. A., Pabon, A., Ladias, J. A. A. & Logothetis, D. E. (1996) J. Gen. Physiol. 107, 381-397.
18. Logothetis, D. E., Movahedi, S., Satler, C., Lindpaintner, K. & Nadal-Ginard, B. (1992) Neuron 8, 531-540.
19. Hamill, O. P., Marty, A., Neher, E., Sakmann, B. & Sigworth, F. J. (1981) Pflügers Arch. 391, 85-100.
20. Methfessel, C., Witzemann, V., Takahashi, T., Mishina, M., Numa, S. & Sakmann, B. (1986) Pflügers Arch. 407, 577-588.
21. Stühmer, W. (1992) Methods Enzymol. 207, 319-339.
22. Vivaudou, M. B., Arnoult, C. & Villaz, M. (1991) J. Membr. Biol. 122, 165-175.
23. Heidbüchel, H., Callewaert, G., Vereecke, J. & Carmeliet, E. (1990) Pflügers Arch. 416, 213-215.
24. Kim, D. (1991) J. Physiol. (London) 437, 133-155.
25. Kurachi, Y., Ito, H., Sugimoto, T., Shimizu, L, Miki, I. & Ui, M. (1989) Nature (London) 337, 555-557.
26. Kim, D., Lewis, L. L., Graziadei, L., Neer, E. J., Bar-Sagi, D. & Clapham, D. E. (1989) Nature (London) 337, 557-560.
27. Huang, C.-L. & Hilgemann, D. W. (1997) Biophys. J. 72, A250.
28. DebBurman, S. K., Ptasienski, J., Benovic, J. L. & Hosey, M. M. (1996) J. Biol. Chem. 271, 22552-22562.
29. Pitcher, J. A., Touhara, K., Payne, E. S. & Lefkowitz, R. J. (1995) J. Biol. Chem. 270, 11707-11710.
30. DebBurman, S. K., Ptasienski, J., Boetticher, E., Lomansney, J. W., Benovic. J. L. & Hosey, M. M. (1995) J. Biol. Chem. 270, 5742-5747.
31. Pitcher, J. A., Fredericks, Z. L., Stone, W. C., Premont, R. T., Stoffel, R. H., Koch, W. J. & Lefkowitz, R. J. (1996) J. Biol. Chem. 271, 24907-24913.
32. Pertile, P., Liscovitch, M., Chalifa, V. & Cantley, L. C. (1995) J. Biol. Chem. 270, 5130-5135.
33. Harlan, J. E., Hajduk, P. J., Yoon, H. S. & Fesik, S. W. (1994) Nature (London) 371, 168-170.
34. Mayer, B. J., Ren, R., Clark, K. L. & Baltimore, D. (1993) Cell 73, 629-630.
35. Touhara, K., Inglese, J., Pitcher, J. A., Shaw, G. & Lefkowitz, R. J. (1994) J. Biol. Chem. 269, 10217-10220.
36. Tsukada, S., Simon, M. I., Witte, O. N. & Katz, A. (1994) Proc. Natl. Acad. Sci. USA 91, 11256-11260.
37. Yao, L., Kawakami, Y. & Kawakami, T. (1994) Proc. Natl. Acad. Sci. USA 91, 9175-9179.
38. Fukami, K., Sawada, N., Endo, T. & Takenawa, T. (1996) J. Biol. Chem. 271, 2646-2650.