丝氨酸38磷酸化对B细胞中活化诱导的胞苷脱氨酶DNA脱氨活性的调节。
Regulation of activation-induced cytidine deaminase DNA deamination activity in B-cells by Ser38 phosphorylation.
作者信息
Basu Uttiya, Franklin Andrew, Schwer Bjoern, Cheng Hwei-Ling, Chaudhuri Jayanta, Alt Frederick W
机构信息
Howard Hughes Medical Institute, Children's Hospital Boston, Boston, MA 02115, USA.
出版信息
Biochem Soc Trans. 2009 Jun;37(Pt 3):561-8. doi: 10.1042/BST0370561.
Human and mouse Ig genes are diversified in mature B-cells by distinct processes known as Ig heavy-chain CSR (class switch recombination) and Ig variable-region exon SHM (somatic hypermutation). These DNA-modification processes are initiated by AID (activation-induced cytidine deaminase), a DNA cytidine deaminase predominantly expressed in activated B-cells. AID is post-transcriptionally regulated via multiple mechanisms, including microRNA regulation, nucleocytoplasmic shuttling, ubiquitination and phosphorylation. Among these regulatory processes, AID phosphorylation at Ser(38) has been a focus of particularly intense study and debate. In the present paper, we discuss recent biochemical and mouse genetic studies that begin to elucidate the functional significance of AID Ser(38) phosphorylation in the context of the evolution of this mode of AID regulation and the potential roles that it may play in activated B-cells during a normal immune response.
人类和小鼠的免疫球蛋白（Ig）基因在成熟B细胞中通过称为Ig重链类别转换重组（CSR）和Ig可变区外显子体细胞超突变（SHM）的不同过程实现多样化。这些DNA修饰过程由激活诱导的胞苷脱氨酶（AID）启动，AID是一种主要在活化B细胞中表达的DNA胞苷脱氨酶。AID通过多种机制进行转录后调控，包括微小RNA调控、核质穿梭、泛素化和磷酸化。在这些调控过程中，AID丝氨酸（Ser）38位点的磷酸化一直是特别深入研究和争论的焦点。在本文中，我们讨论了最近的生化和小鼠遗传学研究，这些研究开始阐明AID丝氨酸38位点磷酸化在AID这种调控模式演变背景下的功能意义，以及它在正常免疫反应期间活化B细胞中可能发挥的潜在作用。
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