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首页> 外文期刊>Journal of Molecular Biology >The Roles of Actin-Binding Domains 1 and 2 in the Calcium-Dependent Regulation of Actin Filament Bundling by Human Plastins
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The Roles of Actin-Binding Domains 1 and 2 in the Calcium-Dependent Regulation of Actin Filament Bundling by Human Plastins

机译：肌动蛋白结合结构域1和2在人塑料中肌动蛋白丝束钙依赖性调节中的作用

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摘要

The actin cytoskeleton is a complex network controlled by a vast array of intricately regulated actin-binding proteins. Human plastins (PLS1, PLS2, and PLS3) are evolutionary conserved proteins that non-covalently crosslink actin filaments into tight bundles. Through stabilization of such bundles, plastins contribute, in an isoform-specific manner, to the formation of kidney and intestinal microvilli, inner ear stereocilia, immune synapses, endocytic patches, adhesion contacts, and invadosomes of immune and cancer cells. All plastins comprise an N-terminal Ca2+-binding regulatory headpiece domain followed by two actin-binding domains (ABD1 and ABD2). Actin bundling occurs due to simultaneous binding of both ABDs to separate actin filaments. Bundling is negatively regulated by Ca2+, but the mechanism of this inhibition remains unknown. In this study, we found that the bundling abilities of PLS1 and PLS2 were similarly sensitive to Ca2+ (pCa(50) similar to 6.4), whereas PLS3 was less sensitive (pCa(50) similar to 5.9). At the same time, all three isoforms bound to F-actin in a Ca2+-independent manner, suggesting that binding of only one of the ABDs is inhibited by Ca2+. Using limited proteolysis and mass spectrometry, we found that in the presence of Ca2+ the EF-hands of human plastins bound to an immediately adjacent sequence homologous to canonical calmodulin-binding peptides. Furthermore, our data from differential centrifugation, FOrster resonance energy transfer, native electrophoresis, and chemical crosslinking suggest that Ca2+ does not affect ABD1 but inhibits the ability of ABD2 to interact with actin. A structural mechanism of signal transmission from Ca2+ to ABD2 through EF-hands remains to be established. (C) 2017 Elsevier Ltd. All rights reserved.
机译：肌动蛋白细胞骨架是由大量错综复杂的肌动蛋白结合蛋白控制的复杂网络。人的塑料（PLS1，PLS2和PLS3）是进化保守蛋白质，其非共价交联肌肽长丝将长丝成紧密束。通过稳定这种束，以同种型特异性方式促使塑料贡献，以形成肾脏和肠道微毛虫，内耳立体，免疫突触，内吞斑，粘附接触和免疫和癌细胞的侵入症。所有塑料包含N-末端CA2 + - 粘接调节凸起，然后是两个肌动蛋白结合结构域（ABD1和ABD2）。发生肌动蛋白捆绑，由于ABDs与肌动蛋白长丝同时结合。捆绑被Ca2 +负调节，但这种抑制的机制仍然未知。在这项研究中，我们发现PLS1和PLS2的捆绑能力与CA2 +（PCA（50）类似于6.4），敏感性（PCA（50）与5.9类似）相似敏感。同时，所有三种同种型以ca2 + - 依赖性方式结合到f-肌动蛋白，表明只有一个ABDS的结合被Ca2 +抑制。使用有限的蛋白水解和质谱法，我们发现在CA2 +存在于与立即相邻的序列与典型钙调蛋白结合肽相同的人塑料的EF手中。此外，我们的数据来自差分离心，饲料共振能量转移，天然电泳和化学交联表明CA2 +不会影响ABD1，但抑制ABD2与肌动蛋白相互作用的能力。通过EF-DALL从CA2 +到ABD2的信号传输的结构机制仍有待确定。 （c）2017 Elsevier Ltd.保留所有权利。

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