The role of protein phosphorylation in the regulation of class switch recombination

Biocell

article

KANO TANABE¹  RYUTARO KAJIHARA² 

[1] Department of Medical Technology, Faculty of Health Science, Kumamoto Health Science University;Department of Biomedical Laboratory Sciences, Faculty of Life Sciences, Kumamoto University;Center for Immunotherapy, Roswell Park Comprehensive Cancer Center

关键词: Antibody;    Kinase;    Phosphatase;    Signal Transduction;   

DOI  :  10.32604/biocell.2020.012740

学科分类：仪器

来源: Biocell

【 摘 要 】

Antibody is an important part of adaptive immune system and is produced only by B cells. There are five main classes (IgM, IgD, IgG, IgA, IgE) and some subclasses in antibodies. IgM and IgD are produced by mature naïve B cells. On the other hand, IgG, IgA and IgE are produced by activated antigen-specific B cells via class switch recombination (CSR). CSR is the irreversible DNA rearrangement from upstream to downstream classes in immunoglobulin heavy chain genes. Co-stimulations of CD40 ligand (CD40L) and cytokines are required for induction of CSR by activating several transcription factors. These signal transduction pathways involve many protein phosphorylation. Phosphorylation or dephosphorylation of cellular protein is an important kind of post-translational protein modification in intracellular signal transduction. In the fact, more than one third of the intracellular proteins are said to be transiently phosphorylated in human. A protein kinase is an enzyme that catalyzes the addition of phosphate to substrate protein. Whereas, a protein phosphatase catalyzes the removal of phosphate from the substrate. This review focuses on the mechanism of CSR controlled by protein phosphorylation and dephosphorylation. We provide the role of protein kinase and phosphatase in the regulation of class switch recombination.

【 授权许可】

CC BY