Lipid-Dependent Membrane Protein Topogenesis

被引:209
作者
Dowhan, William [1 ,2 ]
Bogdanov, Mikhail [1 ]
机构
[1] Univ Texas Houston, Sch Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA
[2] Univ Texas Houston, Sch Med, Ctr Membrane Biol, Houston, TX 77030 USA
基金
美国国家卫生研究院;
关键词
phosphatidylethanolamine; protein topology; positive-inside rule; lactose permease; lipochaperones; TRANSMEMBRANE CONDUCTANCE REGULATOR; TETRACYCLINE RESISTANCE PROTEIN; SIGNAL SEQUENCE ORIENTATION; POSITIVELY CHARGED RESIDUES; ESCHERICHIA-COLI; LACTOSE PERMEASE; ENDOPLASMIC-RETICULUM; ER MEMBRANE; TOPOLOGICAL ORGANIZATION; PHOSPHOLIPID-COMPOSITION;
D O I
10.1146/annurev.biochem.77.060806.091251
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The topology of polytopic membrane proteins is determined by to pogenic 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 domain 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.
引用
收藏
页码:515 / 540
页数:26
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