Supramolecular assemblies and localized regulation of voltage-gated ion channels.
Supramolecular assemblies and localized regulation of voltage-gated ion channels.
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DOI：
10.1152/physrev.00029.2007
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发表时间：
2009-04
影响因子：
33.6
通讯作者：
Hell JW
中科院分区：
文献类型：
--
作者：
Dai S;Hall DD;Hell JW
这篇综述讨论了通过磷酸化对电压门控离子通道的局部调节。相关蛋白激酶、磷酸酶和相关调节蛋白的通道调节的综合数据主要可用于电压门控 Ca2+ 通道，这构成了本次综述的主要焦点。其他电压门控离子通道，特别是 Kv7.1-3 (KCNQ1-3)、大电导和小电导 Ca2+ 激活的 K+ 通道 BK 和 SK2，以及内向整流 K+ 通道 Kir3 也已得到相当程度的研究，并将包括在内。 PKA 对 L 型 Ca2+ 通道 Cav1.2 的调节已得到最彻底的研究，因为它是心脏战斗或逃跑反应的基础。已鉴定出包含 β2 肾上腺素受体、异三聚体 G 蛋白 Gs、腺苷酸环化酶和 PKA 的原型 Cav1.2 信号复合物，支持通过 cAMP 高度定位。 2 型兰尼碱受体以及 AMPA 型和 NMDA 型谷氨酸受体分别与心肌细胞和神经元中的 Cav1.2 非常接近，但独立锚定 PKA、CaMKII 和丝氨酸/苏氨酸磷酸酶 PP1、PP2A 和 PP2B，如详细讨论的。 PKA、PKC、CaMKII、Src 和各种磷酸酶与 Cav1.2 相互作用的结构和功能方面的描述将包括与其他通道（例如兰尼碱受体或离子型谷氨酸受体）的类似相互作用的比较。 Na+ 和 K+ 通道磷酸化复合物的调节将在单独的论文中讨论。因此，这篇综述面向对离子通道调节或激酶、磷酸酶及其上游调节剂的定位感兴趣的读者。
This review addresses the localized regulation of voltage-gated ion channels by phosphorylation. Comprehensive data on channel regulation by associated protein kinases, phosphatases, and related regulatory proteins are mainly available for voltage-gated Ca2+ channels, which form the main focus of this review. Other voltage-gated ion channels and especially Kv7.1-3 (KCNQ1-3), the large- and small-conductance Ca2+-activated K+ channels BK and SK2, and the inward-rectifying K+ channels Kir3 have also been studied to quite some extent and will be included. Regulation of the L-type Ca2+ channel Cav1.2 by PKA has been studied most thoroughly as it underlies the cardiac fight-or-flight response. A prototypical Cav1.2 signaling complex containing the β2 adrenergic receptor, the heterotrimeric G protein Gs, adenylyl cyclase, and PKA has been identified that supports highly localized via cAMP. The type 2 ryanodine receptor as well as AMPA- and NMDA-type glutamate receptors are in close proximity to Cav1.2 in cardiomyocytes and neurons, respectively, yet independently anchor PKA, CaMKII, and the serine/threonine phosphatases PP1, PP2A, and PP2B, as is discussed in detail. Descriptions of the structural and functional aspects of the interactions of PKA, PKC, CaMKII, Src, and various phosphatases with Cav1.2 will include comparisons with analogous interactions with other channels such as the ryanodine receptor or ionotropic glutamate receptors. Regulation of Na+ and K+ channel phosphorylation complexes will be discussed in separate papers. This review is thus intended for readers interested in ion channel regulation or in localization of kinases, phosphatases, and their upstream regulators.
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