Homer and the ryanodine receptor
Homer and the ryanodine receptor
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DOI：
10.1007/s00249-009-0494-1
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发表时间：
2009-12-01
影响因子：
2
通讯作者：
Dulhunty, Angela Fay
中科院分区：
文献类型：
--
作者：
Pouliquin, Pierre;Dulhunty, Angela Fay
Homer 蛋白最近被鉴定为新型高亲和力配体，可通过与靶蛋白中富含脯氨酸的区域结合的 EVH1 结构域来调节心脏和骨骼肌中的兰尼碱受体 (RyR) Ca2+ 释放通道。许多荷马蛋白还可以通过卷曲螺旋结构域进行自缔合，从而实现多聚化。在其他组织中，尤其是神经元中，Homer 将嵌入表面膜的蛋白质锚定到内质网的 Ca2+ 释放通道上，并且可以将膜或胞浆蛋白锚定到细胞骨架上。尽管 Homer 功能的这种锚定方面尚未在肌肉中得到广泛研究，但 RyR 中及其与大量 RyR 离子通道复合体中相互作用的许多蛋白质上存在 Homer 结合的共有序列。在这篇综述中，我们探讨了 Homer 对肌肉和神经元中也涉及 RyR 通道的各种细胞过程做出贡献的潜力。
Homer proteins have recently been identified as novel high-affinity ligands that modulate ryanodine receptor (RyR) Ca2+ release channels in heart and skeletal muscle, through an EVH1 domain which binds to proline-rich regions in target proteins. Many Homer proteins can also self-associate through a coiled-coil domain that allows their multimerisation. In other tissues, especially neurons, Homer anchors proteins embedded in the surface membrane to the Ca2+ release channel in the endoplasmic reticulum and can anchor membrane or cytosolic proteins to the cytoskeleton. Although this anchoring aspect of Homer function has not been extensively investigated in muscle, there are consensus sequences for Homer binding in the RyR and on many of the proteins that it interacts with in the massive RyR ion channel complex. In this review we explore the potential of Homer to contribute to a variety of cell processes in muscle and neurons that also involve RyR channels.