βL-βM loop in the C-terminal domain of G protein-activated inwardly rectifying K+ channels is important for G βγ subunit activation

Journal of Physiology

Volumn 555, Issue 3, 2004, Pages 643-657

  Finley, Melissa ^a   Arrabit, Christine ^a   Fowler, Catherine ^a   Suen, Kai Fai ^a   Slesinger, Paul A ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; CARBACHOL; EPITOPE; GUANINE NUCLEOTIDE BINDING PROTEIN; INWARDLY RECTIFYING POTASSIUM CHANNEL; POTASSIUM ION; PROTEIN SUBUNIT; G PROTEIN BETA GAMMA; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL; G-PROTEIN BETA GAMMA; GLUTAMIC ACID; GLYCINE; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; HISTIDINE; HYBRID PROTEIN; LEUCINE; POTASSIUM CHANNEL; G BETA GAMMA SUBUNIT; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL 2; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL 2.1; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING ASSAY; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE DEPOLARIZATION; CHANNEL GATING; CHIMERA; CONTROLLED STUDY; CYTOPLASM; ENDOCRINE CELL; HEART MUSCLE CELL; HUMAN; HUMAN CELL; IMMUNOCYTOCHEMISTRY; MOUSE; NERVE CELL; NONHUMAN; OOCYTE; POINT MUTATION; POTASSIUM CURRENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; STATISTICAL ANALYSIS; XENOPUS; ANIMAL; CELL LINE; CHEMISTRY; FEMALE; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; BETA L BETA M LOOP; BINDING AFFINITY; BINDING SITE; CYTOPLASMIC DOMAIN; EMBRYO; HEK293 CELL LINE; IN VITRO STUDY; MOLECULAR DYNAMICS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SENSITIVITY ANALYSIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE; FEMALE; G PROTEIN-COUPLED INWARDLY-RECTIFYING POTASSIUM CHANNELS; GLUTAMIC ACID; GLYCINE; GTP-BINDING PROTEIN BETA SUBUNITS; GTP-BINDING PROTEIN GAMMA SUBUNITS; HISTIDINE; HUMANS; LEUCINE; OOCYTES; POINT MUTATION; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; XENOPUS;

EID: 1642565864     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2003.056101     Document Type: Article

References (50)

1. Blednov YA, Stoffel M, Chang SR & Harris RA (2001). Potassium channels as targets for ethanol: Studies of G-protein-coupled inwardly rectifying potassium channel 2 (GIRK2) null mutant mice. J Pharmacol Exp Ther 298, 521-530.
2. + channel subunit. Proc Natl Acad Sci U S A 93, 14193-14198.
3. Changeux J-P & Edelstein S (1998). Allosteric receptors after 30 years. Neuron 21, 959-980.
4. + channels: Implication for Andersen's syndrome. Proc Natl Acad Sci USA 99, 8430-8435.
5. + channels (GIRKs). J Biol Chem 276, 11409-11413.
6. Doupnik CA, Davidson N & Lester HA (1995). The inward rectifier potassium channel family. Curr Opin Neurobiol 5, 268-277.
7. Finley M, Arrabit C, Fowler C & Slesinger PA (2003). Identification of a conserved C-terminal region of Kir3 important for Gβγ activation. In Biophysical Society 47th Annual Meeting. Biophysical Society, San Antonio, Texas.
8. Hamill OP, Marty A, Neher E, Sakmann B & Sigworth FJ (1981). Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflügers Arch 391, 85-100.
9. + channel activity through interactions with the βγ subunits of G proteins. J Biol Chem 277, 6088-6096.
10. He C, Zhang H, Mirshahi T & Logothetis DE (1999). Identification of a potassium channel site that interacts with G protein βγ subunits to mediate agonist-induced signaling. J Biol Chem 274, 12517-12524.
11. + channel subunit that permits GIRK1 expression of IKACh currents in oocytes. Neuron 16, 423-429.
12. Hille B (1992). Ionic Channels of Excitable Membranes. Sinauer Assoc, Sunderland, MA, USA.
13. + channels. J Biol Chem 274, 8639-8648.
14. Huang C-L, Feng S & Hilgemann DW (1998). Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ. Nature 391, 803-806.
15. + channels. FEBS Lett 405, 291-298.
16. + channel is important for channel activation. Neuron 15, 1133-1143.
17. + channel, GIRK1. Biochem Biophys Res Commun 212, 1022-1028.
18. + channels composed of Kir3.2 subunits in dopaminergic neurons of the substantia nigra. J Neurosci 19, 1006-1017.
19. + channel. J Biol Chem 278, 29174-29183.
20. + (GIRK) channels composed of GIRK2 and GIRK3. J Biol Chem 275, 36211-36216.
21. + channel subunits. Neuropharmacology 35, 831-839.
22. + channels. Nat Neurosci 2, 1091-1097.
23. + channel activation. J Biol Chem 273, 16946-16952.
24. Kubo Y, Baldwin TJ, Jan YN & Jan LY (1993a). Primary structure and functional expression of a mouse inward rectifier potassium channel. Nature 362, 127-133.
25. Kubo Y, Reuveny E, Slesinger PA, Jan YN & Jan LY (1993b). Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel. Nature 364, 802-806.
26. Kunkel MT & Peralta EG (1995). Identification of domains conferring G protein regulation on inward rectifier potassium channels. Cell 83, 443-449.
27. + channels in the brain. FEBS Lett 353, 37-42.
28. Lewohl JM, Wilson WR, Mayfield RD, Brozowski SJ, Morrisett RA & Harris RA (1999). G-protein-coupled inwardly rectifying potassium channels are targets of alcohol action. Nat Neurosci 2, 1084-1090.
29. + channel proteins GIRK1 and GIRK2 and their altered expression in weaver brain. J Neurosci 16, 7137-7150.
30. + channel in heart. Nature 325, 321-326.
31. Ma D, Zerangue N, Raab-Graham K, Fried SR, Jan YN & Jan LY (2002). Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart. Neuron 33, 715-729.
32. Nishida M & MacKinnon R (2002). Structural basis of inward rectification. Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution. Cell 111, 957-965.
33. + channel, GIRK. Neuron 33, 87-99.
34. 2+ ions. J General Physiol 114, 673-684.
35. Reuveny E, Slesinger PA, Inglese J, Morales JM, Iniguez-Lluhi JA, Lefkowitz RJ, Bourne HR, Jan YN & Jan LY (1994). Activation of the cloned muscarinic potassium channel by G protein βγ subunits. Nature 370, 143-146.
36. Sadja R, Smadja K, Alagem N & Reuveny E (2001). Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels. Neuron 29, 669-680.
37. Schulte U, Hahn H, Wiesinger H, Ruppersberg JP & Fakler B (1998). pH-dependent gating of ROMK (Kir 1.1) channels involves conformational changes in both N and C termini. J Biol Chem 273, 34575-34579.
38. + channel GIRK2. Proc Natl Acad Sci U S A 94, 923-927.
39. + channels. Biophys J 80, 707-718.
40. + channels. Neuron 16, 321-331.
41. Slesinger PA, Reuveny E, Jan YN & Jan LY (1995). Identification of structural elements involved in G protein gating of the GIRK1 potassium channel. Neuron 15, 1145-1156.
42. + currents in cerebellar granule cells isolated from weaver and Girk2 null mutant mice. Proc Natl Acad Sci U S A 94, 12210-12217.
43. + ions depends on the presence of phosphatidylinositol phosphates. Proc Natl Acad Sci U S A 95, 1307-1312.
44. Tucker SJ & Ashcroft FM (1999). Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2. J Biol Chem 274, 33393-33397.
45. Wickman KD, Iniguez-Lluhl JA, Davenport PA, Taussig R, Krapivinsky GB, Linder ME, Gilman AG & Clapham DE (1994). Recombinant G-protein βγ-subunits activate the muscarinic-gated atrial potassium channel. Nature 368, 255-257.
46. Wickman K, Nemec J, Gendler SJ & Clapham DE (1998). Abnormal heart rate regulation in GIRK4 knockout mice. Neuron 20, 103-114.
47. Yamada M, Inanobe A & Kurachi Y (1998). G protein regulation of potassium ion channels. Pharmacol Rev 50, 723-757.
48. Yi BA, Lin Y, Jan YN & Jan LY (2001). Yeast screen for constitutively active mutant G protein-activated potassium channels. Neuron 29, 657-667.
49. 2 interactions. Nat Cell Biol 1, 183-188.
50. + channels. Proc Natl Acad Sci U S A 98, 6482-6487.