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Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure

Segawa, Katsumori ; Kurata, Sachiko ; Yanagihashi, Yuichi ; Brummelkamp, Thijn R. ; Matsuda, Fumihiko ; Nagata, Shigekazu

Science (American Association for the Advancement of Science), 2014-06, Vol.344 (6188), p.1164-1168 [Periódico revisado por pares]

United States: American Association for the Advancement of Science

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Título:
Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure
Autor: Segawa, Katsumori ; Kurata, Sachiko ; Yanagihashi, Yuichi ; Brummelkamp, Thijn R. ; Matsuda, Fumihiko ; Nagata, Shigekazu
Assuntos: Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; Annexins ; Apoptosis ; B lymphocytes ; Caspases - metabolism ; Cell Line ; Cell lines ; Cell Membrane - enzymology ; Cell membranes ; Cleavage ; Enzymes ; Epithelial cells ; Exposure ; Genetic Testing ; Humans ; Lipids ; Macrophages ; Membrane Proteins - metabolism ; Membrane Transport Proteins ; Membranes ; Phosphatidylserines - metabolism ; Phospholipid Transfer Proteins - genetics ; Phospholipid Transfer Proteins - metabolism ; Phospholipids ; Protein Transport ; Sheep ; Signal transduction ; T lymphocytes
É parte de: Science (American Association for the Advancement of Science), 2014-06, Vol.344 (6188), p.1164-1168
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Phospholipids are asymmetrically distributed in the plasma membrane. This asymmetrical distribution is disrupted during apoptosis, exposing phosphatidylserine (PtdSer) on the cell surface. Using a haploid genetic screen in human cells, we found that ATP11C (adenosine triphosphatase type 11C) and CDC50A (cell division cycle protein 50A) are required for aminophospholipid translocation from the outer to the inner plasma membrane leaflet; that is, they display flippase activity. ATP11C contained caspase recognition sites, and mutations at these sites generated caspase-resistant ATP11C without affecting its flippase activity. Cells expressing caspase-resistant ATP11C did not expose PtdSer during apoptosis and were not engulfed by macrophages, which suggests that inactivation of the flippase activity is required for apoptotic PtdSer exposure. CDC50A-deficient cells displayed PtdSer on their surface and were engulfed by macrophages, indicating that PtdSer is sufficient as an "eat me" signal.
Editor: United States: American Association for the Advancement of Science
Idioma: Inglês

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Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure

Segawa, Katsumori ; Kurata, Sachiko ; Yanagihashi, Yuichi ; Brummelkamp, Thijn R. ; Matsuda, Fumihiko ; Nagata, Shigekazu

United States: American Association for the Advancement of Science

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