| Literature DB >> 8734447 |
J Eichberg1, S Iyer.
Abstract
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.Entities:
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Year: 1996 PMID: 8734447 DOI: 10.1007/bf02527718
Source DB: PubMed Journal: Neurochem Res ISSN: 0364-3190 Impact factor: 3.996