Targeting of ion channels to membrane microdomains:: localization of Kv channels to lipid rafts

被引:147
作者
Martens, JR
O'Connell, K
Tamkun, M [1 ]
机构
[1] Colorado State Univ, Dept Biomed Sci, Ft Collins, CO 80523 USA
[2] Oregon Hlth Sci Univ, Dept Physiol & Pharmacol, Portland, OR 97201 USA
关键词
D O I
10.1016/j.tips.2003.11.007
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Voltage-gated K+ channels are an important determinant of cellular excitability and key components of multiple signal transduction pathways. However, relatively little is known about the mechanisms of K-v channel localization or their membrane partitioning. Lipid rafts are specialized membrane microdomains that are rich in sphingolipids and cholesterol. These rafts have been implicated in the organization of many membrane-associated signaling pathways and are currently the focus of intense interest in the scientific community. Biochemical and functional evidence indicate that K-v channels, in addition to other ion channels, localize to lipid raft microdomains on the cell surface. Although several important questions regarding specific mechanisms of channel localization remain, emerging data indicate that protein-lipid interactions should be considered as a new mechanism of ion channel localization and compartmentation that might permit the therapeutic modulation of channel properties via alteration in membrane lipids.
引用
收藏
页码:16 / 21
页数:6
相关论文
共 59 条
[1]   Cell biology - A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains [J].
Anderson, RGW ;
Jacobson, K .
SCIENCE, 2002, 296 (5574) :1821-1825
[2]   The caveolae membrane system [J].
Anderson, RGW .
ANNUAL REVIEW OF BIOCHEMISTRY, 1998, 67 :199-225
[3]   Plasma membrane voltage-dependent anion channel mediates antiestrogen-activated Maxi Cl- currents in C1300 neuroblastoma cells [J].
Bahamonde, MI ;
Fernández-Fernández, JM ;
Guix, FX ;
Vázquez, E ;
Valverde, MA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (35) :33284-33289
[4]   Lipid matters: nicotinic acetylcholine receptor-lipid interactions (Review) [J].
Barrantes, FJ .
MOLECULAR MEMBRANE BIOLOGY, 2002, 19 (04) :277-284
[5]   Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platforms [J].
Bock, J ;
Szabó, I ;
Gamper, N ;
Adams, C ;
Gulbins, E .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 305 (04) :890-897
[6]   Modulation of the Kv1.3 potassium channel by receptor tyrosine kinases [J].
Bowlby, MR ;
Fadool, DA ;
Holmes, TC ;
Levitan, IB .
JOURNAL OF GENERAL PHYSIOLOGY, 1997, 110 (05) :601-610
[7]  
BRADY JD, IN PRESS MOL PHARM
[8]   Apical sorting of a voltage- and Ca2+-activated K+ channel α-subunit in Madin-Darby canine kidney cells is independent of N-glycosylation [J].
Bravo-Zehnder, M ;
Orio, P ;
Norambuena, A ;
Wallner, M ;
Meera, P ;
Toro, L ;
Latorre, R ;
González, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (24) :13114-13119
[9]   Structure and function of sphingolipid- and cholesterol-rich membrane rafts [J].
Brown, DA ;
London, E .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (23) :17221-17224
[10]   Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes? [J].
Brown, DA ;
London, E .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1997, 240 (01) :1-7