Membrane Phosphatidylserine Regulates Surface Charge and Protein Localization.
摘要：
Electrostatic interactions with negatively charged membranes contribute to the subcellular targeting of proteins with polybasic or cationic domains. Although the anionic phospholipid phosphatidylserine is comparatively abundant, its contribution to the surface charge of individual cellular membranes is unknown, partly because of the lack of reagents to analyze its distribution in intact cells. We developed a biosensor to study the subcellular distribution of phosphotidylserine and found that it binds the cytosotic leaflets of the plasma membrane, as well as endosomes and lysosomes. The negative charge associated with the presence of phosphotidylserine directed proteins with moderately positive charge to the endocytic pathway. More strongly cationic proteins, normally associated with plasma membrane, relocalized to endocytic compartments when the plasma membrane surface charge decreased on calcium influx.
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年份：
2008
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