Membrane Phosphatidylserine Regulates Surface Charge and Protein Localization

来自 Semantic Scholar

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135

作者：

T Yeung，GE Gilbert，J Shi，J Silvius，A Kapus，S Grinstein

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摘要：

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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关键词：

Experimental/ biochemistry bioelectric phenomena biomembrane transport calcium molecular biophysics proteins/ membrane phosphatidylserine surface charge protein localization electrostatic interactions negatively charged membranes subcellular targeting biosensor cytosolic leaflets endosomes lysosomes calcium influx/ A8725D Biological transport cellular and subcellular transmembrane physics A8720E Natural and artificial biomembranes A8728 Bioelectricity A8715D Physical chemistry of biomolecular solutions condensed states