Journal
ANNUAL REVIEW OF BIOCHEMISTRY
Volume 78, Issue -, Pages 515-540Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.77.060806.091251
Keywords
phosphatidylethanolamine; protein topology; positive-inside rule; lactose permease; lipochaperones
Categories
Funding
- National Institutes of Health [GM20478]
- John S. Dunn Research Foundation.
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [F32GM020478, R01GM020478, R37GM020478] Funding Source: NIH RePORTER
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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.
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