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首页> 外文期刊>Journal of Molecular Biology >Organization of Farnesylated, Carboxymethylated KRAS4B on Membranes
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Organization of Farnesylated, Carboxymethylated KRAS4B on Membranes

机译：法金黑化的组织，羧甲基化kras4b在膜上

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Mutations of the Ras proteins HRAS, KRAS4A, KRAS4B, and NRAS are associated with a high percentage of all human cancers. The proteins are composed of highly homologous N-terminal catalytic or globular domains, plus C-terminal hypervariable regions (HVRs). Post-translational modifications of all RAS HVRs helps target RAS proteins to cellular membrane locations where they perform their signaling functions. For the predominant KRAS4 isoform, KRAS4B, post-translational farnesylation and carboxymethylation, along with a patch of HVR basic residues help foster membrane binding. Recent investigations implicate membrane-bound RAS dimers, oligomers, and nanoclusters as landing pads for effector proteins that relay RAS signals. The details of these RAS signaling platforms have not been elucidated completely, in part due to the difficulties in preparing modified proteins. We have employed properly farnesylated and carboxymethylated KRAS4B in lipid monolayer incubations to examine how the proteins assemble on membranes. Our results reveal novel insights into to how KRAS4B may organize on membranes. (C) 2019 Elsevier Ltd. All rights reserved.
机译：RAS蛋白HRAS，KRAS4a，Kras4b和NRA的突变与所有人类癌症的高百分比相关。蛋白质由高同质的N-末端催化剂或球状结构域组成，加上C末端高变区域（HVRS）。所有RAS HVR的翻译后修饰有助于将RAS蛋白靶向它们执行信号功能的蜂窝膜位置。对于主要的KRAS4同种型，KRAS4B，翻译后的法呢基和羧甲基化以及HVR基本残基的蛋白质有助于促进膜结合。最近的研究将膜结合的RAS二聚体，低聚物和纳米团簇占据用于继电器信号的效应蛋白的着陆垫。由于制备改性蛋白质的困难，这些RAS信号平台的细节尚未完全阐明。我们在脂质单层孵育中使用了适当的法牛酸酯和羧甲基化Kras4b，以检查蛋白质如何组装在膜上。我们的结果揭示了克拉斯4B如何组织膜的新颖见解。 （c）2019 Elsevier Ltd.保留所有权利。

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