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Control of transmembrane lipid asymmetry in chromaffin granules by an ATP-dependent protein

Nature volume 340, pages 75–76 (1989)Cite this article

Abstract

THE Ca2+-dependent binding of annexin proteins to secretory granule membranes seems to be involved in the early stage of exocytosis1—3. Binding studies have shown that these proteins have a specificity for phosphatidylserine (PtdS) interfaces4,5. Further-more, aminolipids are necessary for contact and fusion between lipid vesicles6 or between liposomes and chromaffin granules7. Thus, PtdS must be present on the granule outer (cytoplasmic) monolayer. We report here that chromaffin granules possess a mechanism to maintain PtdS orientation, comparable to the ATP-dependent aminophospholipid translocase from human erythrocytes8-14. The translocase, in granules, selectively transports PtdS from the luminal to the cytoplasmic monolayer, provided the incubation medium contains ATP. As this protein shares several properties with the granule vanadate-sensitive ATPase II15,16, we infer that this ATPase, of relative molecular mass 115,000, is the protein responsible for aminophospholipid translocation. This is the first evidence for an ATP-dependent specific phospholipid 'flippase' in intracellular organelles.

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  1. Institut de Biologic Physico-Chimique, 13 rue Pierre et Marie Curie, F75005, Paris, France

    Alain Zachowski, Jean-Pierre Henry & Philippe F. Devaux

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  1. Alain Zachowski
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  2. Jean-Pierre Henry
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  3. Philippe F. Devaux
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Zachowski, A., Henry, JP. & Devaux, P. Control of transmembrane lipid asymmetry in chromaffin granules by an ATP-dependent protein. Nature 340, 75–76 (1989). https://doi.org/10.1038/340075a0

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