Lipid-dependent membrane protein topogenesis.
Lipid-dependent membrane protein topogenesis.
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DOI：
10.1146/annurev.biochem.77.060806.091251
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发表时间：
2009
影响因子：
16.6
通讯作者：
Bogdanov M
中科院分区：
文献类型：
--
作者：
Dowhan W;Bogdanov M
多孔膜蛋白的拓扑结构由蛋白质中的拓扑发生序列、蛋白质-转位相互作用、蛋白质内折叠过程中的相互作用以及蛋白质与脂质环境之间的相互作用决定。跨膜结构域的取向取决于初始组装过程中的膜磷脂组成以及组装后脂质组成的变化。与正-内规则相反的负氨基酸的膜转位电位在很大程度上被磷脂酰乙醇胺的正常存在所抑制，从而解释了正残基作为保留信号的优势。磷脂酰乙醇胺提供适当的电荷密度，允许膜表面在膜转位和保留信号之间保持电荷平衡，也允许蛋白质细胞质表面存在负性残基用于其他目的。
The topology of polytopic membrane proteins is determined by topogenic sequences in the protein, protein-translocon interactions, and interactions during folding within the protein and between the protein and the lipid environment. Orientation of transmembrane domains is dependent on membrane phospholipid composition during initial assembly as well as on changes in lipid composition postassembly. The membrane translocation potential of negative amino acids working in opposition to the positive-inside rule is largely dampened by the normal presence of phosphatidylethanolamine, thus explaining the dominance of positive residues as retention signals. Phosphatidylethanolamine provides the appropriate charge density that permits the membrane surface to maintain a charge balance between membrane translocation and retention signals and also allows the presence of negative residues in the cytoplasmic face of proteins for other purposes.