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C elegans mitochondrial factor WAH-1 pro ... phospholipid scramblase SCRM-1
C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1.
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Externalization of phosphatidylserine, which is normally restricted to the inner leaflet of plasma membrane, is a hallmark of mammalian apoptosis. It is not known what activates and mediates the phosphatidylserine externalization process in apoptotic cells. Here, we report the development of an annexin V-based phosphatidylserine labelling method and show that a majority of apoptotic germ cells in Caenorhabditis elegans have surface-exposed phosphatidylserine, indicating that phosphatidylserine externalization is a conserved apoptotic event in worms. Importantly, inactivation of the gene encoding either the C. elegans apoptosis-inducing factor (AIF) homologue (WAH-1), a mitochondrial apoptogenic factor, or the C. elegans phospholipid scramblase 1 (SCRM-1), a plasma membrane protein, reduces phosphatidylserine exposure on the surface of apoptotic germ cells and compromises cell-corpse engulfment. WAH-1 associates with SCRM-1 and activates its phospholipid scrambling activity in vitro. Thus WAH-1, after its release from mitochondria during apoptosis, promotes plasma membrane phosphatidylserine externalization through its downstream effector, SCRM-1.
Wang X, Wang J, Gengyo-Ando K, Gu L, Sun CL, Yang C, Shi Y, Kobayashi T, Shi Y, Mitani S, Xie XS, Xue D
Nature cell biology
2007-05-01 00:00
9
5
541-9
Animals,Annexin A5,Apoptosis,Biological Transport,Caenorhabditis elegans,Caenorhabditis elegans Proteins,Caspases,Cell Membrane,Germ Cells,Membrane Proteins,Mitochondria,Mitochondrial Proteins,Models, Molecular,Mutation,Phosphatidylserines,Phospholipid Transfer Proteins,RNA Interference,Staining and Labeling,Time Factors,Annexin A5,CED-2 protein, C elegans,Caenorhabditis elegans Proteins,Membrane Proteins,Mitochondrial Proteins,Phosphatidylserines,Phospholipid Transfer Proteins,SCRM-1 protein, C elegans,Wah-1 protein, C elegans,ced-1 protein, C elegans,Caspases,ced-3 protein, C elegans
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA
Nat. Cell Biol.
1465-7392
10.1038/ncb1574
ncb1574
1355
True
17401362
