AI Article Synopsis
- Electrostatic interactions with negatively charged membranes play a crucial role in directing proteins with positive charge towards specific cellular locations.
- Researchers developed a biosensor to analyze the distribution of the anionic phospholipid phosphatidylserine within intact cells, discovering its presence in the cytosolic leaflets of the plasma membrane as well as in endosomes and lysosomes.
- The study found that the negative charge of phosphatidylserine influences the localization of moderately cationic proteins to the endocytic pathway, while stronger cationic proteins tend to relocate to endocytic compartments when the plasma membrane's charge is altered.
Article Abstract
Electrostatic interactions with negatively charged membranes contribute to the subcellular targeting of proteins with polybasic clusters 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 phosphatidylserine and found that it binds the cytosolic leaflets of the plasma membrane, as well as endosomes and lysosomes. The negative charge associated with the presence of phosphatidylserine directed proteins with moderately positive charge to the endocytic pathway. More strongly cationic proteins, normally associated with the plasma membrane, relocalized to endocytic compartments when the plasma membrane surface charge decreased on calcium influx.
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| http://dx.doi.org/10.1126/science.1152066 | DOI Listing |
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