扩展C2结构域家族：蛋白激酶Cδ、ε、η、θ、磷脂酶、GAP和穿孔素中的C2结构域
Extending the C2 domain family: C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin.
作者信息
Ponting C P, Parker P J
机构信息
University of Oxford, Fibrinolysis Research Unit, United Kingdom.
出版信息
Protein Sci. 1996 Jan;5(1):162-6. doi: 10.1002/pro.5560050120.
Abstract
Various membrane lipid metabolites, generated by phospholipases C and D (PLCs, PLDs), are known to regulate the activities of protein kinases C (PKCs) and GTP-ase activating proteins (GAPs) in a range of cellular processes. Conventional Ca(2+)-dependent PKCs (alpha, beta I, beta II, and gamma), PLCs and various GAPs are all known to contain copies of a phospholipid-binding domain, termed C2 or CalB. Here we recognize that C2 domains are also present in "new" Ca(2+)-independent PKCs (delta, epsilon, eta, and theta), other kinases, a eukaryotic PLD, the breakpoint cluster region (BCR) gene product, and two further GAPS. Twenty-two previously unrecognized C2 domain sequences are presented, which include a single copy in the mammalian poreforming proteins, perforin.
摘要
已知由磷脂酶C和D（PLCs、PLDs）产生的各种膜脂代谢物在一系列细胞过程中调节蛋白激酶C（PKCs）和GTP酶激活蛋白（GAPs）的活性。传统的钙依赖性PKCs（α、βI、βII和γ）、PLCs和各种GAPs都已知含有一个称为C2或钙结合蛋白（CalB）的磷脂结合结构域的拷贝。在这里，我们认识到C2结构域也存在于“新的”钙非依赖性PKCs（δ、ε、η和θ）、其他激酶、一种真核PLD、断裂点簇集区（BCR）基因产物以及另外两种GAPs中。本文给出了22个以前未被识别的C2结构域序列，其中包括在哺乳动物成孔蛋白穿孔素中的一个拷贝。
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