Mass spectrometry-based phosphoproteomics reveals multisite phosphorylation on mammalian brain voltage-gated sodium and potassium channels

被引:27
作者
Baek, Hyun [1 ]
Cerda, Oscar [1 ]
Trimmer, James S. [1 ,2 ]
机构
[1] Univ Calif Davis, Dept Neurobiol Physiol & Behav, Davis, CA 95616 USA
[2] Univ Calif Davis, Dept Physiol & Membrane Biol, Davis, CA 95616 USA
关键词
Mass spectrometry; Phosphoproteomics; VGSC (Nav channel); VGKC (Kv channel); Brain ion channel; DEPENDENT PROTEIN-KINASE; K+ CHANNELS; ION CHANNELS; FUNCTIONAL IMPLICATIONS; PROTEOMIC ANALYSIS; ALPHA-SUBUNITS; KV2.1; CHANNEL; NA+ CHANNELS; IN-VIVO; MODULATION;
D O I
10.1016/j.semcdb.2010.09.009
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Voltage-gated sodium and potassium channels underlie electrical activity of neurons, and are dynamically regulated by diverse cell signaling pathways that ultimately exert their effects by altering the phosphorylation state of channel subunits. Recent mass spectrometric-based studies have led to a new appreciation of the extent and nature of phosphorylation of these ion channels in mammalian brain. This has allowed for new insights into how neurons dynamically regulate the localization, activity and expression through multisite ion channel phosphorylation. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:153 / 159
页数:7
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