Identification of an erythroid ATP-dependent aminophospholipid transporter.
The asymmetric distribution of amino-containing phospholipids in plasma membranes is essential for the function and survival of mammalian cells. Phosphatidylserine (PS) is restricted to the inner leaflet of plasma membranes by an ATP-dependent transport process. Exposure of PS on the surface of cells serves as a binding site for haemostatic factors, triggers cell-cell interaction and recognition by macrophages and phospholipases. Exposure of PS on the red cell surface plays a significant role in sickle cell pathology. We report the identification of two different isoforms of the aminophospholipid translocase, Atp8a1, or flippase, in the murine red blood cell membrane.
Soupene
Eric
E
Children's Hospital Oakland Research Institute, Martin Luther King Jr Way, Oakland, CA 94609, USA. esoupene@chori.org
Kuypers
Frans A
FA
D000251:Adenosine Triphosphatases / Q000097:blood* / Q000235:genetics; D000255:Adenosine Triphosphate / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D004910:Erythrocyte Membrane / Q000737:chemistry*; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D049294:Phospholipid Transfer Proteins / Q000097:blood* / Q000235:genetics; D012313:RNA / Q000235:genetics; D016415:Sequence Alignment
D049294:Phospholipid Transfer Proteins; D012313:RNA; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C510547:Atp8a1 protein, mouse