A subfamily of P-type ATPases with aminophospholipid transporting activity

被引:413
作者
Tang, XJ
Halleck, MS
Schlegel, RA
Williamson, P
机构
[1] AMHERST COLL,DEPT BIOL,AMHERST,MA 01002
[2] PENN STATE UNIV,DEPT BIOCHEM & MOLEC BIOL,UNIVERSITY PK,PA 16802
关键词
D O I
10.1126/science.272.5267.1495
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The appearance of phosphatidylserine on the surface of animal cells triggers phagocytosis and blood coagulation. Normally, phosphatidylserine is confined to the inner leaflet of the plasma membrane by an aminophospholipid translocase, which has now been cloned and sequenced. The bovine enzyme is a member of a previously unrecognized subfamily of P-type adenosine triphosphatases (ATPases) that may have diverged from the primordial enzyme before the separation of the known families of ion-translocating ATPases. Studies in Saccharomyces cerevisiae suggest that aminophospholipid translocation is a general function of members of this family.
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页码:1495 / 1497
页数:3
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