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Science 319 (5860): 210-213

Copyright © 2008 by the American Association for the Advancement of Science

Membrane Phosphatidylserine Regulates Surface Charge and Protein Localization

Tony Yeung,1 Gary E. Gilbert,2 Jialan Shi,2 John Silvius,3 Andras Kapus,4 Sergio Grinstein1*

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.

1 Division of Cell Biology, The Hospital for Sick Children, Toronto M5G 1X8, Canada.
2 Department of Medicine, Department of Veterans Affairs, VA Boston Healthcare System, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
3 Department of Biochemistry, McGill University, Montreal H3G 1Y6, Canada.
4 Keenan Research Center in the Li Ka Sheng Knowledge Institute of St. Michael's Hospital and Department of Surgery, University of Toronto, Toronto M5B 1W8, Canada.

* To whom correspondence should be addressed. E-mail: sga{at}sickkids.ca


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Crystal Structure of Lactadherin C2 Domain at 1.7A Resolution with Mutational and Computational Analyses of Its Membrane-binding Motif.
C. Shao, V. A. Novakovic, J. F. Head, B. A. Seaton, and G. E. Gilbert (2008)
J. Biol. Chem. 283, 7230-7241
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