Identification and purification of aminophospholipid flippases

被引：163

作者：

Daleke, DL ^{[1
]}

Lyles, JV

机构：

[1] Indiana Univ, Dept Biochem & Mol Biol, Bloomington, IN 47405 USA

[2] Indiana Univ, Med Sci Program, Bloomington, IN 47405 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2000年 / 1486卷 / 01期

基金：

美国国家卫生研究院;

关键词：

phospholipid transport; phosphatidylserine; ATPase; flippase;

D O I：

10.1016/S1388-1981(00)00052-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transbilayer phospholipid asymmetry is a common structural feature of most biological membranes. This organization of lipids is generated and maintained by a number of phospholipid transporters that vary in lipid specificity, energy requirements and direction of transport. These transporters can be divided into three classes: (1) bidirectional, non-energy dependent 'scramblases', and energy-dependent transporters that move lipids (2) toward ('flippases') or (3) away from ('floppases') the cytofacial surface of the membrane. One of the more elusive members of this family is the plasma membrane aminophospholipid flippase, which selectively transports phosphatidylserine from the external to the cytofacial monolayer of the plasma membrane. This review summarizes the characteristics of aminophospholipid flippase activity in intact cells and describes current strategies to identify and isolate this protein. The biochemical characteristics of candidate flippases are critically compared and their potential role in flippase activity is evaluated. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：108 / 127

页数：20

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