PHOSPHORYLATION OF MYELIN PROTEINS - RECENT ADVANCES

Authors
Citation
J. Eichberg et S. Iyer, PHOSPHORYLATION OF MYELIN PROTEINS - RECENT ADVANCES, Neurochemical research, 21(4), 1996, pp. 527-535
Citations number
84
Categorie Soggetti
Biology,Neurosciences
Journal title
ISSN journal
03643190
Volume
21
Issue
4
Year of publication
1996
Pages
527 - 535
Database
ISI
SICI code
0364-3190(1996)21:4<527:POMP-R>2.0.ZU;2-D
Abstract
Since it was first described 25 years ago, phosphorylation has come to be recognized as a widespread and dynamic post-translational modifica tion of myelin proteins. In this review, the phosphorylation character istics of myelin basic protein, protein zero (P-0), myelin-associated glycoprotein and 2'3' cyclic nucleotide 3'-phosphodiesterase are summa rized. Emphasis is placed on recent advances in our knowledge concerni ng the protein kinases involved and the sites of phosphorylation in th e amino acid sequences, where known. The possible roles of myelin prot ein phosphorylation in modulating myelin structure, the process of mye lin assembly and mediation of signal transduction events are discussed .