Phosphorylation of myelin-associated glycoprotein in vivo and in vitro occurs only in the cytoplasmic domain of the large isoform.
Myelin-associated glycoprotein (MAG) was radioactively labelled with 32P both in intact brain and in myelin membrane preparations. Chemical deglycosylation of the phosphorylated products revealed that only one of the MAG isoforms (L-MAG) is labelled in vitro. Furthermore, the phosphorylation events in vivo and in vitro are confined to the cytoplasmic portion of the L-MAG isoform. Tryptic mapping of L-MAG labelled both in vivo and in vitro revealed that the majority of the sites phosphorylated in intact brain are also phosphorylated in myelin membrane preparations; however, the extent of phosphorylation at individual sites is variable. The results demonstrate that partially purified myelin membrane preparations can be used to study the enzymes responsible for MAG phosphorylation and dephosphorylation events in vivo.
Edwards
A M
AM
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Braun
P E
PE
Bell
J C
JC
D000818:Animals; D002855:Chromatography, Thin Layer; D003593:Cytoplasm / Q000378:metabolism; D006031:Glycosylation; D007163:Immunosorbent Techniques; D018993:Myelin P0 Protein; D009185:Myelin Proteins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D014357:Trypsin / Q000378:metabolism
D018993:Myelin P0 Protein; D009185:Myelin Proteins; D014357:Trypsin