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首页> 外文期刊>Molecular and Cellular Biology >CD2AP Regulates SUMOylation of CIN85 in Podocytes
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CD2AP Regulates SUMOylation of CIN85 in Podocytes

机译：CD2AP调节足细胞中CIN85的SUMOylation

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Podocytes are highly differentiated and polarized epithelial cells located on the visceral side of the glomerulus. They form an indispensable component of the glomerular filter, the slit diaphragm, formed by several transmembrane proteins and adaptor molecules. Disruption of the slit diaphragm can lead to massive proteinuria and nephrotic syndrome in mice and humans. CD2AP is an adaptor protein that is important for the maintenance of the slit diaphragm. Together with its paralogue, CIN85, CD2AP belongs to a family of adaptor proteins that are primarily described as being involved in endocytosis and downregulation of receptor tyrosine kinase activity. We have shown that full-length CIN85 is upregulated in podocytes in the absence of CD2AP, whereas in wild-type cells, full-length CIN85 is not detectable. In this study, we show that full-length CIN85 is postranslationally modified by SUMOylation in wild-type podocytes. We can demonstrate that CIN85 is SUMOylated by SUMO-1, -2, and -3 and that SUMOylation is enhanced in the presence of CD2AP. Conversion of lysine 598 to arginine completely abolishes SUMOylation and leads to increased binding of CIN85 to nephrin. Our results indicate a novel role for CD2AP in regulating posttranslational modification of CIN85.
机译：足细胞是位于肾小球内脏侧的高度分化和极化的上皮细胞。它们形成了肾小球滤膜的必不可少的组成部分，即裂隙膜，它是由几种跨膜蛋白和衔接子分子形成的。裂隙隔膜破裂会导致小鼠和人类大量蛋白尿和肾病综合征。 CD2AP是一种衔接蛋白，对维持裂隙隔膜很重要。 CD2AP及其旁系同源蛋白CIN85属于衔接子蛋白家族，主要被描述为参与胞吞作用和受体酪氨酸激酶活性的下调。我们已经表明，在不存在CD2AP的情况下，足细胞中的全长CIN85被上调，而在野生型细胞中，全长CIN85是不可检测的。在这项研究中，我们表明全长CIN85在野生型足细胞中被SUMOylation进行了翻译后修饰。我们可以证明CIN85被SUMO-1，-2和-3 SUMO化，并且CD2AP存在时SUMOylation增强。赖氨酸598向精氨酸的转化完全消除了SUMOylation，并导致CIN85与nephrin的结合增加。我们的结果表明CD2AP在调节CIN85的翻译后修饰中具有新作用。

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