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Description

Myelin basic protein (UniProt: also known as MBP) is encoded by the MBP gene in guinea pig. MBP is a homodimeric protein that is found in both the central and the peripheral nervous system. It is one of the most abundant protein component of the myelin membrane in the CNS and plays a role in both the formation and stabilization of this myelin membrane. It is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. At least 5 charge isomers (C1, C2, C3, C4, and C5) are reported to be produced because of optional post-translational modifications such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues. Of these C1 isomer is the most cationic, least modified, and most abundant form and C5 is the least cationic form. C1 and C2 are reported to be unphosphorylated, C3 and C4 are monophosphorylated, and C5 is phosphorylated at two positions. Phosphorylation is achieved with the help of TAOK2, VRK2, MAPK11, MAPK12, MAPK14, and MINK1). MBP can interact with many polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and with negatively charged lipids. (Ref.: Boggs, JM (2006). Cell. Mol. Life Sci. 63(17), 1945-61).