STRONG VOLTAGE-DEPENDENT INWARD RECTIFICATION OF INWARD RECTIFIER K+ CHANNELS IS CAUSED BY INTRACELLULAR SPERMINE

被引:312
作者
FAKLER, B [1 ]
BRANDLE, U [1 ]
GLOWATZKI, E [1 ]
WEIDEMANN, S [1 ]
ZENNER, HP [1 ]
RUPPERSBERG, JP [1 ]
机构
[1] UNIV TUBINGEN HOSP, EAR NOSE & THROAT CLIN, DEPT SENSORY BIOPHYS, D-72076 TUBINGEN, GERMANY
关键词
D O I
10.1016/0092-8674(95)90459-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Inward rectifier K+ channels mediate the K+ conductance at resting potential in many types of cell. Since these K+ channels do not pass outward currents (inward rectification) when the cell membrane is depolarized beyond a trigger threshold, they play an important role in controlling excitability. Both a highly voltage-dependent block by intracellular Mg2+ and an endogenous gating process are presently assumed to underly inward rectification. It is shown that strong voltage dependence of rectification found under physiological conditions is predominantly due to the effect of intracellular spermine. Physiological concentrations of free spermine mediate strong rectification of IRK1 inward rectifier K+ channels even in the absence of free Mg2+ and in IRK1 mutant channels that have no endogenous rectification.
引用
收藏
页码:149 / 154
页数:6
相关论文
共 50 条
[41]   Modulation of inward-rectifier K+ channels by epimers of cholesterol in BAEC [J].
Romanenko, VG ;
Rothblat, GH ;
Levitan, I .
BIOPHYSICAL JOURNAL, 2002, 82 (01) :28A-28A
[42]   Pharmacological implications of inward rectifier K+ channels regulation by cytoplasmic polyamines [J].
Taglialatela, M ;
Ficker, E ;
Wible, B ;
Brown, AM .
PHARMACOLOGICAL RESEARCH, 1995, 32 (06) :335-344
[43]   Gating dependence of inner pore access in inward rectifier K+ channels [J].
Phillips, LR ;
Enkvetchakul, D ;
Nichols, CG .
NEURON, 2003, 37 (06) :953-962
[44]   Merging functional studies with structures of inward-rectifier K+ channels [J].
Delphine Bichet ;
Friederike A. Haass ;
Lily Yeh Jan .
Nature Reviews Neuroscience, 2003, 4 :957-967
[45]   The Site for Docking Cations in Cytoplasmic Domain of Inward Rectifier K+ Channels [J].
Inanobe, Atsushi ;
Nakagawa, Atsushi ;
Kurachi, Yoshihisa .
BIOPHYSICAL JOURNAL, 2010, 98 (03) :697A-697A
[46]   The site for docking cations in cytoplasmic domain of inward rectifier K+ channels [J].
Inanobe, Atsushi ;
Nakagawa, Atsushi ;
Kurachi, Yoshihisa .
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2010, 112 :237P-237P
[47]   Merging functional studies with structures of inward-rectifier K+ channels [J].
Bichet, D ;
Haass, FA ;
Jan, LY .
NATURE REVIEWS NEUROSCIENCE, 2003, 4 (12) :957-967
[48]   Interaction between cations and cytoplasmic domain of inward rectifier K+ channels [J].
Inanobe, Atsushi ;
Nakagawa, Atsushi ;
Kurachi, Yoshihisa .
JOURNAL OF PHYSIOLOGICAL SCIENCES, 2010, 60 :S82-S82
[49]   Inward rectification of the AKT2 channel abolished by voltage-dependent phosphorylation [J].
Michard, E ;
Dreyer, I ;
Lacombe, B ;
Sentenac, H ;
Thibaud, JB .
PLANT JOURNAL, 2005, 44 (05) :783-797
[50]   Kir4.1/Kir5.1 channels possess strong intrinsic inward rectification determined by a voltage-dependent K+-flux gating mechanism [J].
Marmolejo-Murillo, Leticia G. ;
Arechiga-Figueroa, Ivan A. ;
Moreno-Galindo, Eloy G. ;
Ferrer, Tania ;
Zamora-Cardenas, Rodrigo ;
Navarro-Polanco, Ricardo A. ;
Sanchez-Chapula, Jose A. ;
Rodriguez-Menchaca, Aldo A. .
JOURNAL OF GENERAL PHYSIOLOGY, 2021, 153 (05)