A subfamily of P-type ATPases with aminophospholipid transporting activity
A subfamily of P-type ATPases with aminophospholipid transporting activity
复制标题
DOI：
10.1126/science.272.5267.1495
复制
发表时间：
1996-06-07
期刊：
影响因子：
56.9
通讯作者：
Williamson, P
中科院分区：
文献类型：
--
作者：
Tang, XJ;Halleck, MS;Williamson, P
磷脂酰丝氨酸在动物细胞表面的出现触发吞噬作用和血液凝固。通常情况下，磷脂酰丝氨酸被限制在质膜的内部小叶的氨基磷脂移位酶，现在已经被克隆和测序。牛酶是以前未被认识的P型腺苷三磷酸酶（ATP酶）亚家族的成员，该亚家族可能在已知的离子转运ATP酶家族分离之前从原始酶中分离出来。在酿酒酵母中的研究表明，氨基磷脂易位是该家族成员的一般功能。
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.