Lint Johan Van, Rykx An, Vantus Tibor, Vandenheede Jackie R
Division of Biochemistry, Faculty of Medicine, Campus Gasthuisberg, Katholieke Universiteit Leuven, Leuven, B-3000, Leuven, Belgium.
Int J Biochem Cell Biol. 2002 Jun;34(6):577-81. doi: 10.1016/s1357-2725(01)00163-7.
The protein kinase D (PKD) enzymes represent a new family of second messenger stimulated kinases, with diacylglycerol as a prime, but not the sole, mediator of activation. Their molecular architecture features a catalytic domain, unrelated to that of all PKC family members, and a large inhibitory, regulatory domain, comprised of two Zinc fingers, and a pleckstrin homology domain. These different sub-domains play distinctive roles in the activation, translocation and biological functions of the kinase. The enzymes have been implicated in signalling mechanisms controlling cell proliferation and programmed cell death and in metastasis, immune responses, and Golgi restructuring and function. A variety of proteins specifically interact with the different sub-domains of the enzymes and direct their wide range of cellular functions.
蛋白激酶D（PKD）酶代表了一类新的第二信使刺激型激酶，二酰基甘油是其主要但并非唯一的激活介质。它们的分子结构特征包括一个与所有蛋白激酶C（PKC）家族成员不同的催化结构域，以及一个由两个锌指和一个普列克底物蛋白同源结构域组成的大的抑制性调节结构域。这些不同的亚结构域在激酶的激活、易位和生物学功能中发挥着独特作用。这些酶参与了控制细胞增殖、程序性细胞死亡以及转移、免疫反应和高尔基体重组与功能的信号传导机制。多种蛋白质与这些酶的不同亚结构域特异性相互作用，并指导其广泛的细胞功能。
