Enzymatic Methylation of Arginine Residue in Myelin Basic Protein

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

“…Thus, although we consider that PTMs modulate MBP's conformation, even highly-modified MBP is still an IUP that, on its own, would not attain a defined fold driven by formation of a hydrophobic core. Brostoff and Eylar (1971), Baldwin and Carnegie (1971a,b), Chanderkar et al (1986), Kim et al (1988Kim et al ( , 2003 and Pritzker et al (2000b) 108-GLSLS-112 113 Arg R Potentially deiminated Wood et al (1996) 114 Phe F 115 Ser S Phosphorylated Turner et al (1984), Kishimoto et al (1985) and Kim et al (2003) 116-WGAEG-120 121 Gln Q Deamidated Kim et al (2003) 122 Arg R Deiminated Wood and Moscarello (1989) and Kim et al (2003) 123-PGFGYGG-129 130 Arg R Deiminated Wood and Moscarello (1989) and Kim et al (2003) 131-ASDYK-135 136 Ser S Phosphorylated Kishimoto et al (1985) 137-AHKGFKGVDA-146 147 Gln Q Deamidated Chou et al (1976), Zand et al (1998) and Kim et al (2003) 148 Gly G 149 Thr T Phosphorylated Kim et al (2003) 150 Leu L 151 Ser S Phosphorylated Kishimoto et al (1985) and Kim et al (2003) 152-KIFKLGG-158 159 Arg R Deiminated; methylated Wood and Moscarello (1989) and Kim et al (2003) 160 Asp D 161 Ser S Phosphorylated Kishimoto et al (1985) and Zand et al (1998) Kishimoto et al (1985), Zand et al (1998) and Kim et al (2003) 166-PMA-168 169 Arg R Potentially deiminated Wood et al (1996) 170 Arg R Deiminated Wood and Moscarello (1989) Data have been adapted from and Wood and Moscarello (1997), with addition of more recent data from Kim et al (2003). In extreme cases of fulminating MS, arginyl residues at potentially all sites can be deiminated (W...…”

Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosisThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease.

“…In contrast, a significant change in the distribution of exII-MBP isoforms from the pellet to the supernatant fractions occurred with aging. The methylation of MBP (at Arg104 in 18.5 kDa murine MBP) is correlated with compact myelin, and stabilizes the protein's structure and protects it from proteolysis (Chanderkar et al 1986;Kim et al 1988;Rawal et al 1992;Pritzker et al 2000). During myelination, exII-MBPs are translocated into the nucleus, where they may have a regulatory role (Pedraza et al 1997).…”