Functional Analysis of PKC Phosphorylation Sites on Myelin Protein Zero

• 作者: GangXu JanneBalsamo JohnKamhoz MichaelShy
• 来源期刊: 临床医药杂志
• 学科: 生物学
• 关键词: 髓磷脂蛋白质基点 蛋白激酶C 磷酸化 RSTK 外周神经系统
• 年，卷（期）: lcyyzz_2003,（4）
• 页码范围: 1-7
• 页数: 7页
• 分类号: Q55

摘要

Objective To analyze the function of Protein kinase C(PKC) phosphorylation sites on mylelin protein zero (P0) at adhesion and myelination.Methods Mutations of p0 cyto-plasmic domain motif (RSTK) and adjacent sequence which are targeted by PKC were studied.Results The point mutations in this region or an adjacent serine residue could abolish P0 adhe-sion function. PKCα,along with the PKC binding protein RACK1,were associated with wild type P0.Inhibition of PKC activity abolished the P0 mediated adhesion.Point mutation in the RSTKtarget site that abolished adhesion did not alter the association of PKC with P0,but deletion of a 14 amino acid region,which included the PSTK motif,could abolish the association.Conclusion PKC mediated phosphorylation of specific residues within the cytoplasmic domain of P0 is neces-sary for P0 mediated adhesion.The alteration of this phoporylation can cause demyelinating neu-ropathy in human.