The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation
The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation
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DOI：
10.1021/bi101343p
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发表时间：
2010-12-21
期刊：
影响因子：
2.9
通讯作者：
Albanesi, Joseph P.
中科院分区：
文献类型：
--
作者：
Barylko, Barbara;Wang, Lei;Albanesi, Joseph P.
动力蛋白在胞吞作用和高尔基体出芽过程中诱导膜囊泡形成，这一过程需要组装依赖性GT3激活。大脑特异性发动蛋白1比普遍表达的发动蛋白2具有更弱的自组装和自激活倾向。在这里，我们表明，发动蛋白3，这在神经元突触中具有重要的功能，共享的自组装和GT3激活的发动蛋白2的特性。动力蛋白杂合体和动力蛋白I、动力蛋白2和动力蛋白1、动力蛋白3杂聚物的分析揭示，浓度依赖性GTdR活化被动力蛋白1的C-末端脯氨酸/脯氨酸富集结构域抑制。发动蛋白脯氨酸/富含脯氨酸的结构域也介导与含有SH 3结构域的蛋白质的相互作用，从而调节发动蛋白的自缔合和异缔合。
Dynamins induce membrane vesiculation during endocytosis and Golgi budding in a process that requires assembly-dependent GTPase activation. Brain-specific dynamin 1 has a weaker propensity to self-assemble and self-activate than ubiquitously expressed dynamin 2. Here we show that dynamin 3, which has important functions in neuronal synapses, shares the self-assembly and GTPase activation characteristics of dynamin 2. Analysis of dynamin hybrids and of dynamin I dynamin 2 and dynamin 1 dynamin 3 heteropolymers reveals that concentration-dependent GTPase activation is suppressed by the C-terminal proline/arginine-rich domain of dynamin 1. Dynamin proline/arginine-rich domains also mediate interactions with SH3 domain-containing proteins and thus regulate both self-association and heteroassociation of dynamins.