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Science 11 January 2008:
Vol. 319. no. 5860, pp. 210 - 213
DOI: 10.1126/science.1152066
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Reports

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*

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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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The "Electrostatic-Switch" Mechanism: Monte Carlo Study of MARCKS-Membrane Interaction.
S. Tzlil, D. Murray, and A. Ben-Shaul (2008)
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Thematic Review Series: Glycerolipids. Phosphatidylserine and phosphatidylethanolamine in mammalian cells: two metabolically related aminophospholipids.
J. E. Vance (2008)
J. Lipid Res. 49, 1377-1387
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Identification of Regions Required for Apical Membrane Localization of Human Multidrug Resistance Protein 2.
P. E. Bandler, C. J. Westlake, C. E. Grant, S. P. C. Cole, and R. G. Deeley (2008)
Mol. Pharmacol. 74, 9-19
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Annexin A6-induced Inhibition of Cytoplasmic Phospholipase A2 Is Linked to Caveolin-1 Export from the Golgi.
L. Cubells, S. V. de Muga, F. Tebar, J. V. Bonventre, J. Balsinde, A. Pol, T. Grewal, and C. Enrich (2008)
J. Biol. Chem. 283, 10174-10183
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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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Science. ISSN 0036-8075 (print), 1095-9203 (online)