Phosphorylation of myelin protein: recent advances.
Since it was first described 25 years ago, phosphorylation has come to be recognized as a widespread and dynamic post-translation modification of myelin proteins. In this review, the phosphorylation characteristics of myelin basic protein, protein zero (P0), myelin-associated glycoprotein and 2'3' cyclic nucleotide 3'-phosphodiesterase are summarized. Emphasis is placed on recent advances in our knowledge concerning the protein kinases involved and the sites of phosphorylation in the amino acid sequences, where known. The possible roles of myelin protein phosphorylation in modulating myelin structure, the process of myelin assembly and mediation of signal transduction events are discussed.
Eichberg
J
J
Department of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934, USA.
Iyer
S
S
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D006023:Glycoproteins / Q000737:chemistry; D004676:Myelin Basic Protein / Q000737:chemistry; D009185:Myelin Proteins / Q000737:chemistry*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D015398:Signal Transduction
D006023:Glycoproteins; D004676:Myelin Basic Protein; D009185:Myelin Proteins; D011494:Protein Kinases; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases