Dynamic regulation potassium channel of the voltage-gated Kv2.1 by multisite phosphorylation
Dynamic regulation potassium channel of the voltage-gated Kv2.1 by multisite phosphorylation
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DOI：
10.1042/bst0351064
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发表时间：
2007-11-01
影响因子：
3.9
通讯作者：
Trimmer, J. S.
中科院分区：
文献类型：
--
作者：
Mohapatra, D. P.;Park, K. -S.;Trimmer, J. S.
电压门控性K+通道是神经元兴奋性的关键调节器。Kv2.1电压门控K+通道是在大多数中枢神经元中表达的主要延迟整流K+通道，其作为高度磷酸化的蛋白质存在。Kv2.1通过其活性和钙调神经磷酸酶依赖性去磷酸化在内源性神经元兴奋性的稳态调节中起关键作用。在这里，我们回顾研究导致在体内Kv2.1磷酸化位点，其中一个子集有助于电压依赖性门控的分级调制的识别和功能表征。这些研究结果表明，不同的发育，细胞和状态特异性调节磷酸化在特定的网站赋予Kv2.1的功能多样性，这是至关重要的，它作为一个调节器的内在神经元兴奋性的作用。
Voltage-gated K+ channels are key regulators of neuronal excitability. The Kv2.1 voltage-gated K+ channel is the major delayed rectifier K+ channel expressed in most central neurons, where it exists as a highly phosphorylated protein. Kv2.1 plays a critical role in homoeostatic regulation of intrinsic neuronal excitability through its activity- and calcineurin-dependent dephosphorylation. Here, we review studies leading to the identification and functional characterization of in vivo Kv2.1 phosphorylation sites, a subset of which contribute to graded modulation of voltage-dependent gating. These findings show that distinct developmental-, cell- and state-specific regulation of phosphorylation at specific sites confers a diversity of functions on Kv2.1 that is critical to its role as a regulator of intrinsic neuronal excitability.