Phospholipid flippase activities and substrate specificities of human type IV P-type ATPases localized to the plasma membrane.

H. Takatsu,Gaku Tanaka,Katsumori Segawa,Jun Suzuki,S. Nagata,K. Nakayama,Hye-Won Shin

Published 2016 in Journal of Biological Chemistry

ABSTRACT

Type IV P-type ATPases (P4-ATPases) are believed to translocate aminophospholipids from the exoplasmic to the cytoplasmic leaflets of cellular membranes. The yeast P4-ATPases, Drs2p and Dnf1p/Dnf2p, flip NBD-labeled phosphatidylserine (PS) at the Golgi complex and NBD-labeled phosphatidylcholine (PC) at the plasma membrane, respectively. However, the flippase activities and substrate specificities of mammalian P4-ATPases remain incompletely characterized. In this study, we established an assay for phospholipid flippase activities of plasma membrane–localized P4-ATPases using human cell lines stably expressing ATP8B1, ATP8B2, ATP11A, and ATP11C. We found that ATP11A and ATP11C have flippase activities towards PS and

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