The recent discovery and structure determination of a novel ubiquitin-like dimerization domain in protein kinase D (PKD) has significant implications for its activation. PKD is a serine/threonine kinase activated by the lipid second messenger diacylglycerol (DAG). It is an essential and highly conserved protein that is implicated in plasma membrane directed trafficking processes from the trans-Golgi network. However, many open questions surround its mechanism of activation, its localization, and its role in the biogenesis of cargo transport carriers. In reviewing this field, the focus is primarily on the mechanisms that control the activation of PKD at precise locations in the cell. In light of the new structural findings, the understanding of the mechanisms underlying PKD activation is critically evaluated, with particular emphasis on the role of dimerization in PKD autophosphorylation, and the provenance and recognition of the DAG that activates PKD.

中文翻译：

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探戈需要两个步骤：通过二聚作用激活蛋白激酶D。

在蛋白激酶D（PKD）中新型泛素样二聚化结构域的最新发现和结构确定对其激活具有重要意义。PKD是由脂质第二信使二酰基甘油（DAG）激活的丝氨酸/苏氨酸激酶。它是一种重要且高度保守的蛋白质，与反式高尔基体网络的质膜定向运输过程有关。然而，许多悬而未决的问题围绕着其激活机制，定位及其在货物运输载体的生物发生中的作用。在回顾该领域时，重点主要放在控制细胞中精确位置的PKD激活的机制上。根据新的结构发现，我们对对PKD激活的基本机制的理解进行了严格评估，