Phospholipid-flipping activity of P4-ATPase drives membrane curvature

  • EMBO J. 2018 May 2;37(9):e97705. doi: 10.15252/embj.201797705.
Naoto Takada  1 ,  Tomoki Naito  1 ,  Takanari Inoue  2 ,  Kazuhisa Nakayama  1 ,  Hiroyuki Takatsu  1 ,  Hye-Won Shin  3
Affiliations
  • 1. Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.
  • 2. Department of Cell Biology, Center for Cell Dynamics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
  • 3. Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan [email protected].
PMID: 29599178 DOI: 10.15252/embj.201797705
Abstract

P4-ATPases are phospholipid flippases that translocate Phospholipids from the exoplasmic/luminal to the cytoplasmic leaflet of biological membranes. All P4-ATPases in yeast and some in Other organisms are required for membrane trafficking; therefore, changes in the transbilayer lipid composition induced by flippases are thought to be crucial for membrane deformation. However, it is poorly understood whether the phospholipid-flipping activity of P4-ATPases can promote membrane deformation. In this study, we assessed membrane deformation induced by flippase activity via monitoring the extent of membrane tubulation using a system that allows inducible recruitment of Bin/amphiphysin/Rvs (BAR) domains to the plasma membrane (PM). Enhanced phosphatidylcholine-flippase activity at the PM due to expression of ATP10A, a member of the P4-ATPase family, promoted membrane tubulation upon recruitment of BAR domains to the PM This is the important evidence that changes in the transbilayer lipid composition induced by P4-ATPases can deform biological membranes.

Keywords
BAR domain; curvature; flippase; lipid; plasma membrane.