Eichberg J, Iyer S
Department of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934, USA.
Neurochem Res. 1996 Apr;21(4):527-35. doi: 10.1007/BF02527718.
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.
自25年前首次被描述以来，磷酸化已被公认为是髓鞘蛋白广泛且动态的翻译后修饰。在这篇综述中，总结了髓鞘碱性蛋白、零蛋白（P0）、髓鞘相关糖蛋白和2',3'-环核苷酸3'-磷酸二酯酶的磷酸化特征。重点介绍了我们在已知的参与的蛋白激酶和氨基酸序列中的磷酸化位点方面的最新知识进展。还讨论了髓鞘蛋白磷酸化在调节髓鞘结构、髓鞘组装过程和信号转导事件介导中的可能作用。
