메뉴 건너뛰기
Current Opinion in Neurobiology
Volumn 5, Issue 3, 1995, Pages 268-277
The inward rectifier potassium channel family
Author keywords

[No Author keywords available]
Indexed keywords

MAGNESIUM ION; POLYAMINE; POTASSIUM; POTASSIUM CHANNEL;
EID: 0029015089     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/0959-4388(95)80038-7     Document Type: Article
Times cited : (411)
References (86)
  • 1
    • 0001390390 scopus 로고
    • Les constantes électriques de la membrane du muscle
    • (1949) Arch Sci Physiol , vol.3 , pp. 285-299
    • Katz1
  • 2
    • 0027537268 scopus 로고
    • Cloning and expression of an inwardly rectifying ATP-regulated potassium channel
    • of outstanding interest, First molecular description of a Kir channel in the literature. Kir1.1 (ROMK1) was isolated by expression cloning in Xenopus oocytes from a rat outer medullary kidney cDNA library.
    • (1993) Nature , vol.362 , pp. 31-38
    • Ho1    Nichols2    Lederer3    Lytton4    Vassilev5    Kanazirska6    Hebert7
  • 3
    • 0027403280 scopus 로고
    • Primary structure and functional expression of a mouse inward rectifier potassium channel
    • of outstanding interest, Using expression cloning strategies similar to Ho et al. [2], the steeply rectifying Kir2.1 channel (IRK1) that is expressed in a murine macrophage cell line was isolated. A noted level of sequence similarity between Kir2.1 and Kir1.1 provided the first indication of a new Kir channel gene family.
    • (1993) Nature , vol.362 , pp. 127-133
    • Kubo1    Baldwin2    Jan3    Jan4
  • 5
    • 0027219695 scopus 로고
    • Primary structure and functional expression of a rat G protein-coupled muscarinic potassium channel
    • of outstanding interest, The authors isolated Kir3.1 (GIRK1) by homology screening with the Kir2.1 (IRK1) clone. See also annotation [4].
    • (1993) Nature , vol.364 , pp. 802-806
    • Kubo1    Reuveny2    Slesinger3    Jan4    Jan5
  • 6
    • 0027746155 scopus 로고
    • Molecular cloning, functional expression and localization of an inward rectifier potassium channel in the mouse brain
    • of special interest, In situ hybridization study on expression patterns of Kir2.1 in the mouse brain. By using antisense probes to the unique 3′ untranslated region of Kir2.1, the authors avoided cross-hybridization with subsequently cloned Kir2.0 subfamily members and other Kir channels. The mouse Kir2.1 gene was mapped to chromosome 11.
    • (1993) FEBS Lett , vol.336 , pp. 375-380
    • Morishige1    Takahashi2    Findlay3    Koyama4    Zanelli5    Peterson6    Jenkins7    Copeland8    Mori9    Kurachi10
  • 7
    • 0028033103 scopus 로고
    • Gating mechanism of the cloned inward rectifier potassium channel from mouse heart
    • (1994) J Membr Biol , vol.142 , pp. 55-64
    • Ishihara1    Hiraoka2
  • 13
    • 0027959625 scopus 로고
    • + channels in the brain
    • of special interest, Using low stringency hybridization to Kir3.1, the authors isolated novel G-protein-gated Kir channels expressed in mouse brain, indicating the presence of a Kir3.0 subfamily.
    • (1994) FEBS Letters , vol.353 , pp. 37-42
    • Lesage1    Duprat2    Fink3    Guillemare4    Coppola5    Lazdunski6    Hugnot7
  • 14
    • 0028150803 scopus 로고
    • Cloning and expression of a family of inward rectifier potassium channels
    • of special interest, Degenerate primers towards the highly conserved Kir channel P-region were used to amplify novel Kir channel clones from a rat brain cDNA library. Kir4.1 and Kir5.1 were identified, as well as Kir2.3. Kir4.1 and Kir5.1, which constitute potentially new Kir channel subfamilies as they have low sequence identity with other Kir channels.
    • (1994) Recept Channels , vol.2 , pp. 183-191
    • Bond1    Pessia2    Xia3    Lagrutta4    Kavanaugh5    Adelman6
  • 16
    • 0028298653 scopus 로고
    • Cloning a novel human brain inward rectifier potassium channel and its functional expression in Xenopus oocytes
    • (1994) FEBS Lett , vol.348 , pp. 239-243
    • Tang1    Yang2
  • 18
    • 0028144742 scopus 로고
    • ATP channel
    • ATP channels has been subsequently challenged with the demonstration that Kir3.4 co-assembles with Kir3.1 in atrial cell membranes to form the native muscarinic Kir channel. See annotation [65].
    • (1994) Nature , vol.370 , pp. 456-459
    • Ashford1    Bond2    Blair3    Adelman4
  • 21
    • 0027380629 scopus 로고
    • Structure-function studies on the pore of potassium channels
    • (1993) J Membr Biol , vol.136 , pp. 1-8
    • Pongs1
  • 24
    • 0027377896 scopus 로고
    • Nomenclature for mammalian potassium channel genes
    • of special interest, The authors propose a standardized nomenclature for Kir channels, similar to that introduced for voltage-gated Kv channels.
    • (1993) Trends Pharmacol Sci , vol.14 , pp. 434
    • Chandy1    Gutman2
  • 27
    • 0028108544 scopus 로고
    • A conductance maximum observed in an inward rectifier potassium channel
    • of outstanding interest, An elegant biophysical analysis of the permeation and pore properties of Kir1.1. The authors observed a single-channel conductance maximum, which is expected for a single-file multi-ion pore and predicted for Kir channels [26].
    • (1994) J Gen Physiol , vol.104 , pp. 477-486
    • Lu1    MacKinnon2
  • 30
    • 0028061201 scopus 로고
    • Cloning and characterization of multiple forms of the human kidney ROM-K potassium channel
    • of special interest, These two recent studies [29,30] characterized the human Kir1.1 splice variants. An additional exon (exon 4) was identified by Shuck et al. [30], which was not present in the human Kir1.1 cDNA isoforms isolated by Yano et al. [29].
    • (1994) J Biol Chem , vol.269 , pp. 24261-24270
    • Shuck1    Bock2    Benjamin3    Tsai4    Lee5    Slightom6    Bienkowski7
  • 31
    • 0027951056 scopus 로고
    • Primary structure and functional properties of an epithelial K channel
    • (1994) Am J Physiol , vol.266 , pp. C809-C824
    • Zhou1    Tate2    Palmer3
  • 33
    • 0020647563 scopus 로고
    • Fast inward-rectifying current accounts for anomalous rectification in olfactory cortex neurones
    • (1983) J Physiol (Lond) , vol.335 , pp. 153-178
    • Constanti1    Galvan2
  • 34
    • 0024241098 scopus 로고
    • Somatostatin induces an inward rectification in rat locus coeruleus neurones through a pertussis toxin-sensitive mechanism
    • (1988) J Physiol (Lond) , vol.407 , pp. 177-198
    • Inoue1    Nakajima2    Nakajima3
  • 36
    • 0027184270 scopus 로고
    • Inward-rectifying potassium channels in retinal glial (Muller) cells
    • (1993) J Neurosci , vol.13 , pp. 3333-3345
    • Newman1
  • 37
    • 0019393868 scopus 로고
    • Inward rectification in frog skeletal muscle fibres and its dependence on membrane potential and external potassium
    • (1981) J Physiol (Lond) , vol.319 , pp. 295-309
    • Leech1    Stanfield2
  • 38
    • 0021286987 scopus 로고
    • Conductance properties of single inwardly rectifying potassium channels in ventricular cells from guinea-pig heart
    • (1984) J Physiol (Lond) , vol.347 , pp. 641-657
    • Sakmann1    Trube2
  • 39
    • 0022270902 scopus 로고
    • Voltage-dependent activation of the inward-rectifier potassium channel in the ventricular cell membrane of guinea-pig heart
    • (1985) J Physiol (Lond) , vol.366 , pp. 365-385
    • Kurachi1
  • 42
    • 0025823735 scopus 로고
    • Inwardly rectifying potassium current in mammalian lens epithelial cells
    • (1991) Am J Physiol , vol.261 , pp. C115-C123
    • Cooper1    Rae2    Dewey3
  • 43
    • 0023814377 scopus 로고
    • Inwardly rectifying whole-cell and single-channel K currents in the murine macrophage cell line J744.1
    • (1988) J Membr Biol , vol.103 , pp. 41-53
    • McKinney1    Gallin2
  • 44
    • 0026520645 scopus 로고
    • Inwardly rectifying potassium current in rabbit osteoclasts: a whole-cell and single-channel study
    • (1992) J Membr Biol , vol.126 , pp. 171-181
    • Kelly1    Dixon2    Sims3
  • 47
    • 0028942817 scopus 로고
    • A G protein-gated K channel is activated via β2-adrenergic receptors and Gβγ subunits in Xenopus oocytes
    • of special interest, Although β-adrenergic receptor activation of G-protein-gated Kir channels is not known to occur naturally, this paper demonstrates that under appropriate heterologous conditions, the Gβγ subunit released by ligand binding to the β2-adrenergic receptor can activate Kir3.1. These findings raise questions regarding the mechanisms of receptor specificity for Gβγ activation of Kir3.1.
    • (1995) J Gen Physiol , vol.105 , pp. 421-439
    • Lim1    Dascal2    Labarca3    Davidson4    Lester5
  • 49
    • 0028322077 scopus 로고
    • Activation of the cloned muscarinic potassium channel by G protein βγ subunits
    • of outstanding interest, Using heterologous expression of cloned G proteins and Kir3.1 in Xenopus oocytes, the authors demonstrate that Gβγ subunits activate Kir3.1, whereas Gα subunits do not. These studies provide compelling evidence that Gβγ dimers, and not Gα subunits, gate the native channel. Lack of activation in a Kir3.1 mutant subtype with a truncated carboxyl terminus suggests Gβγ coupling at the carboxyl terminus.
    • (1994) Nature , vol.370 , pp. 143-146
    • Reuveny1    Slesinger2    Inglese3    Morales4    Iniguez-Lluhi5    Lefkowitz6    Bourne7    Jan8    Jan9
  • 50
    • 0027983609 scopus 로고
    • + channel critical for activation by G protein βγ subunits
    • 2 subunits. Unfortunately, the electrophysiological properties of this chimera were not studied in detail. The presented data indicate a chimeric channel with weak inward rectification, a property uncharacteristic of either of the donor channels.
    • (1994) Neuron , vol.13 , pp. 747-755
    • Takao1    Yoshii2    Kanda3    Kokubun4    Nukada5
  • 55
    • 0029062203 scopus 로고
    • Contributions of the C-terminal domain to gating properties of inward rectifier potassium channels
    • of special interest, A Kir channel chimera consisting of the amino-terminal and transmembrane domains of Kir4.1 together with the carboxy-terminal end of Kir3.1, was found to transfer certain properties of Kir3.1 to Kir4.1. Unlike the Kir2.1/3.1 chimera of Takao et al. [50], the carboxyl terminus of Kir3.1 did not transfer G-protein gating onto Kir4.1. However, the characteristic slow voltage-dependent gating of Kir3.1 was successfully transferred to Kir4.1. It is postulated that the carboxyl terminus of Kir3.1 is an intrinsic blocking particle analogous to the amino-terminal inactivation ball of Shaker Kv1.1 channels.
    • (1995) Neuron
    • Pessia1    Bond2    Kavanaugh3    Adelman4
  • 56
    • 0028363444 scopus 로고
    • Human G-protein-coupled inwardly rectifying potassium channel (GIRK1) gene (KCNJ3): localization to chromosome 2 and identification of a simple tandem repeat polymorphism
    • (1994) Genomics , vol.21 , pp. 254-256
    • Stoffel1    Espinosa2    Powell3    Philipson4    LeBeau5    Bell6
  • 58
    • 0028606460 scopus 로고
    • G protein-activated inwardly rectifying potassium channel (GIRK1/KGA) mRNA in adult rat heart and brain by in situ hybridization histochemistry
    • (1994) Mol Cell Neurosci , vol.5 , pp. 515-522
    • DePaoli1    Bell2    Stoffel3
  • 60
  • 62
    • 0028111939 scopus 로고
    • A second subunit of the olfactory cyclic nucleotide-gated channel confers high sensitivity to cAMP
    • (1994) Neuron , vol.13 , pp. 611-621
    • Liman1    Buck2
  • 65
    • 0028934859 scopus 로고
    • + channel proteins
    • of special interest. of outstanding interest, First demonstration of a heteromultimeric Kir channel complex in native tissue. Kir3.1-specific antibodies were used to immunoprecipitate the native channel from atrial membranes. Co-precipitating with the 56 kDa Kir3.1 protein (after deglycosylation), was a 45 kDa protein determined by microsequencing and cloning to be Kir3.4 [18]. Co-expression of Kir3.1 and Kir3.4 in several heterologous expression systems produced functional Kir channels that were G-protein-gated by either agonist activation of co-expressed M2 muscarinic receptors, or directly with purified Gβγ dimers applied to inside-out membrane patches. Heterodimeric Kir3.1/3.4 channels display single-channel kinetic properties that more closely resemble those of the native atrial channel, more so than homomeric Kir3.1 or Kir3.4 channels.
    • (1995) Nature , vol.374 , pp. 135-141
    • Krapivinsky1    Gordon2    Wickman3    Velimirovic4    Krapivinsky5    Clapham6
  • 67
    • 0028225248 scopus 로고
    • + channels
    • of outstanding interest, A structure/function study on multiple Kir1.1/Kir2.1 chimeras aimed at mapping the domain(s) mediating Kir2.1's steep inward rectification. The major structural element of Kir2.1 that determined steep inward rectification was identified as the carboxyl terminus. Later findings of the aspartic acid residue in M2 of Kir2.1 as a major determinant of channel block and gating suggests that Kir2.1 may have multiple interaction sites with cytoplasmic blockers.
    • (1994) Science , vol.264 , pp. 844-847
    • Taglialatela1    Wible2    Caporaso3    Brown4
  • 68
    • 0028181693 scopus 로고
    • 2+-dependent inward rectification of ROMK1 potassium channels expressed in Xenopus oocytes
    • (1994) J Physiol (Lond) , vol.476 , pp. 399-409
    • Nichols1    Ho2    Hebert3
  • 69
    • 0028168240 scopus 로고
    • + channel
    • of outstanding interest, To date, the most detailed mutational analysis of the M2 blocking site. All possible amino acids were introduced at this site in Kir1.1, and their effects on inward rectification quantitatively assessed.
    • (1994) Nature , vol.371 , pp. 243-246
    • Lu1    MacKinnon2
  • 71
    • 0023930982 scopus 로고
    • Open-state substructure of inwardly rectifying potassium channels revealed by magnesium block in guinea-pig heart cells
    • (1988) J Physiol (Lond) , vol.397 , pp. 237-258
    • Matsuda1
  • 73
    • 0027984375 scopus 로고
    • Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification
    • of outstanding interest, See annotation [74].
    • (1994) Nature , vol.372 , pp. 366-369
    • Lopatin1    Makhina2    Nichols3
  • 74
    • 0028028412 scopus 로고
    • + channels to intracellular spermine
    • of outstanding interest, Three recent studies [72–74] are the first descriptions of intracellular polyamine block on several Kir channel clones, including M2 mutants. Together they provide compelling evidence that polyamines play an important role in Kir channel function, and indicate an extrinsic mechanism for ‘intrinsic’ Kir channel gating.
    • (1994) FEBS Lett , vol.356 , pp. 199-203
    • Fakler1    Brandle2    Bond3    Glowatzki4    Koenig5    Adelman6    Zenner7    Ruppersberg8
  • 76
    • 0027978279 scopus 로고
    • + channels localized to a single negatively charged residue
    • of special interest, See annotation [77].
    • (1994) Nature , vol.371 , pp. 246-249
    • Wible1    Taglialatela2    Ficker3    Brown4
  • 83
    • 0028670803 scopus 로고
    • + channels are regulated independently by protein kinases and ATP hydrolysis
    • 2+, protein kinase A, and protein kinase C on Kir2.1 activity are carefully assessed.
    • (1994) Neuron , vol.13 , pp. 1413-1420
    • Fakler1    Brandle2    Glowatzki3    Zenner4    Ruppersberg5
  • 86

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.