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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Assembly and dynamics of proteins of the longitudinal and junctional sarcoplasmic reticulum in skeletal muscle cells
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Assembly and dynamics of proteins of the longitudinal and junctional sarcoplasmic reticulum in skeletal muscle cells

机译：骨骼肌细胞中纵向和交界肌质网蛋白的组装和动力学

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摘要

The sarcoplasmic reticulum (SR) of skeletal muscle cells is a complex network of tubules and cisternae that share a common lumen delimited by a single continuous membrane. The SR contains longitudinal and junctional domains characterized by distinctive patterns of protein localization, but how SR proteins reach and/or are retained at these sites is not known. Here, we report that the organization of longitudinal SR proteins is a slow process characterized by temporally distinct patterns of protein localization. In contrast, junctional SR proteins rapidly and synchronously assembled into clusters which, however, merged into mature triadic junctions only after completion of longitudinal SR protein organization. Fluorescence recovery after photobleaching experiments indicated that SR organization was accompanied by significant changes in the dynamic properties of longitudinal and junctional proteins. The decrease in mobility that accompanied organization of the longitudinal SR proteins ank1.5-GFP and GFP-InsP3R1 was abrogated by deletion of specific binding sites for myofibrillar or cytoskeletal proteins, respectively. Assembly of junctional SR domains was accompanied by a strong decrease in mobility of junctional proteins that in triadin appeared to be mediated by its intraluminal region. Together, the data suggest that the organization of specific SR domains results from a process of membrane reorganization accompanied by the establishment of multiple protein-protein interactions with intrinsic and extrinsic cues.
机译：骨骼肌细胞的肌质网（SR）是由肾小管和水箱组成的复杂网络，它们共享由单个连续膜分隔的共同管腔。 SR包含以蛋白质定位的独特模式为特征的纵向和连接结构域，但是SR蛋白如何到达和/或保留在这些位点尚不清楚。在这里，我们报告纵向SR蛋白的组织是一个缓慢的过程，其特征是蛋白定位的时间上不同。相反，接合SR蛋白迅速且同步地组装成簇，然而，只有在完成纵向SR蛋白组织后，这些SR蛋白才融合成成熟的三联体接合。光漂白实验后的荧光恢复表明，SR组织伴随着纵向和连接蛋白动力学特性的显着变化。伴随着纵向SR蛋白ank1.5-GFP和GFP-InsP3R1的组织而发生的运动性降低，通过分别删除了肌原纤维或细胞骨架蛋白的特异性结合位点而被消除。连接SR结构域的组装伴随着连接蛋白迁移率的强烈降低，在三联蛋白中似乎由其管腔内区域介导。总之，数据表明特定SR结构域的组织是由膜重组过程伴随着与内在和外在线索的多种蛋白质-蛋白质相互作用的建立而产生的。

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