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J. Biol. Chem., Vol. 277, Issue 22, 19876-19881, May 31, 2002

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Loss of Plasma Membrane Phospholipid Asymmetry Requires Raft Integrity
ROLE OF TRANSIENT RECEPTOR POTENTIAL CHANNELS AND ERK PATHWAY^*

Corinne Kunzelmann-Marche, Jean-Marie Freyssinet, and M. Carmen Martínez

From the Institut d'Hématologie et d'Immunologie, Université Louis Pasteur, Faculté de Médecine, 4 rue Kirschleger, 67085 Strasbourg, France and the Unité 143 INSERM, Hôpital de Bicêtre, 94275 Le Kremlin-Bicêtre, France

Cholesterol-rich membrane microdomains, also termed lipid rafts, are implicated in the recruitment of essential proteins for intracellular signal transduction. In nonstimulated cells, phosphatidylserine, an anionic aminophospholipid essential for the hemostatic response, is mostly sequestered in the inner leaflet of the plasma membrane. Cell stimulation by Ca²⁺-mobilizing or apoptogenic agents induces the migration of phosphatidylserine to the exoplasmic leaflet, allowing the assembly and activation of several key enzyme complexes of the coagulation cascade and phagocyte recognition of stimulated or senescent cells. We have recently proposed that store-operated Ca²⁺ entry regulates externalization of phosphatidylserine at the cell surface (Kunzelmann-Marche, C., Freyssinet, J.-M., and Martínez, M. C. (2001) J. Biol. Chem. 276, 5134-5139). Here, we show that store-operated Ca²⁺ entry and phosphatidylserine exposure are dramatically reduced after raft disruption by methyl--cyclodextrin. In addition, transient receptor potential channel 1-specific antibody was able to significantly decrease Ca²⁺-induced redistribution of phosphatidylserine. Furthermore, store-operated Ca²⁺ entry and phosphatidylserine exposure were dependent in part on the extracellular signal-regulated kinase pathway associated with rafts. Hence, raft integrity and store-operated Ca²⁺ entry involving transient receptor potential channel 1 channels are essential for completion of the phosphatidylserine transmembrane redistribution process.

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