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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >α-Actinin2 cytoskeletal protein is required for the functional membrane localization of a Ca~(2+)-activated K~+ channel (SK2 channel)
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α-Actinin2 cytoskeletal protein is required for the functional membrane localization of a Ca~(2+)-activated K~+ channel (SK2 channel)

机译：Ca-（2+）激活的K〜+通道（SK2通道）的功能膜定位需要α-Actinin2细胞骨架蛋白

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摘要

The importance of proper ion channel trafficking is underpinned by a number of channel-linked genetic diseases whose defect is associated with failure to reach the cell surface. Conceptually, it is reasonable to suggest that the function of ion channels depends critically on the precise subcellular localization and the number of channel proteins on the cell surface membrane, which is determined jointly by the secretory and endocytic pathways. Yet the precise mechanisms of the entire ion channel trafficking pathway remain unknown. Here, we directly demonstrate that proper membrane localization of a small-conductance Ca~(2+)-activated K~+ channel (SK2 or K_(Ca)2.2) is dependent on its interacting protein, α-actinin2, a major F-actin crosslinking protein. 5K2 channel localization on the cell-surface membrane is dynamically regulated, and one of the critical steps includes the process of cytoskeletal anchoring of SK2 channel by its interacting protein, α-actinin2, as well as endocytic recycling via early endosome back to the cell membrane. Consequently, alteration of these components of SK2 channel recycling results in profound changes in channel surface expression. The importance of our findings may transcend the area of K~+ channels, given that similar cytoskeletal interaction and anchoring may be critical for the membrane localization of other ion channels in neurons and other excitable cells.
机译：适当的离子通道运输的重要性受到许多与通道相关的遗传疾病的支持，这些疾病的缺陷与无法到达细胞表面有关。从概念上讲，合理的建议是离子通道的功能主要取决于精确的亚细胞定位和细胞表面膜上通道蛋白的数量，这由分泌和内吞途径共同决定。然而，整个离子通道迁移途径的确切机制仍然未知。在这里，我们直接证明小电导Ca〜（2+）激活的K〜+通道（SK2或K_（Ca）2.2）的正确膜定位取决于其相互作用蛋白α-actinin2，主要是F-肌动蛋白交联蛋白。 5K2通道在细胞表面膜上的定位是动态调节的，关键步骤之一包括SK2通道通过其相互作用蛋白α-actinin2锚定细胞骨架的过程，以及通过早期内体循环回到细胞膜的内吞再循环。因此，SK2通道再循环这些组分的改变导致通道表面表达的深刻变化。鉴于相似的细胞骨架相互作用和锚定对于神经元和其他可兴奋细胞中其他离子通道的膜定位可能至关重要，因此我们发现的重要性可能会超越K +通道的范围。

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    Ling Lu; Valeriy Timofeyev; Ning Li; Sassan Rafizadeh; Anil Singapuri; Todd R. Harris; Nipavan Chiamvimonvat;

  • 作者单位

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616 College of Life Sciences, Nanjing Normal University, Nanjing 210046, China;

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616;

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616;

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616;

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616;

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616;

    Division of Cardiovascular Medicine, Department of Medicine, University of California, Davis, CA 95616 Department of Veterans Affairs, Northern California Health Care System, Mather, CA 95655 Division of Cardiovascular Medicine,Department of Medicine, University of California, Davis, One Shields Avenue, GBSF 6315,Davis, CA 95616;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    ion channel trafficking; early endosome; cardiac myocytes; small conductance Ca~(2+)-activated K~+ channel; calmodulin binding domain;

    机译：离子通道运输;早期内体心肌细胞小电导Ca〜（2+）激活的K〜+通道;钙调蛋白结合结构域;

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