共 91 条
Functions of phospholipid flippases
被引:78
作者:

Tanaka, Kazuma
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机构:
Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan

Fujimura-Kamada, Konomi
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h-index: 0
机构:
Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan

Yamamoto, Takaharu
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机构:
Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan
机构:
[1] Hokkaido Univ, Div Mol Interact, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan
基金:
日本学术振兴会;
关键词:
Cdc50;
flippase;
phospholipid asymmetry;
P-type ATPase;
vesicle transport;
P-TYPE ATPASE;
YEAST PLASMA-MEMBRANE;
INTRAHEPATIC CHOLESTASIS TYPE-1;
CHROMAFFIN GRANULE MEMBRANES;
EXCHANGE FACTORS GEA1P;
SACCHAROMYCES-CEREVISIAE;
AMINOPHOSPHOLIPID TRANSLOCASE;
ENDOPLASMIC-RETICULUM;
RETROGRADE TRANSPORT;
CANALICULAR MEMBRANE;
D O I:
10.1093/jb/mvq140
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
070307 [化学生物学];
071010 [生物化学与分子生物学];
摘要:
Asymmetrical distribution of phospholipids is generally observed in the eukaryotic plasma membrane. Maintenance and changes of this phospholipid asymmetry are regulated by ATP-driven phospholipid translocases. Accumulating evidence indicates that type 4 P-type ATPases (P4-ATPases, also called flippases) translocate phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of the plasma membrane and internal membranes. Among P-type ATPases, P4-ATPases are unique in that they are associated with a conserved membrane protein of the Cdc50 family as a non-catalytic subunit. Recent studies indicate that flippases are involved in various cellular functions, including transport vesicle formation and cell polarity. In this review, we will focus on the functional aspect of phospholipid flippases.
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页码:131 / 143
页数:13
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