Tomoki Naito

TL;DR: It is shown that endoplasmic reticulum (ER)-anchored lipid transfer proteins, the GRAMD1s, sense and transport accessible PM cholesterol to the ER, and facilitate the movement of accessible PMolesterol to theER in order to counteract an acute increase of PM cholesterol, thereby activating non-vesicular cholesterol transport.

TL;DR: The ARF1+ARF4 and ARF3 pairs are both required for integrity of recycling endosomes but are involved in distinct transport pathways: the former pair regulates retrograde transport from endosome to the TGN, whereas the latter is required for the transferrin recycling pathway from endOSomes to the plasma membrane.

TL;DR: The results suggest that enhanced PC flipping activity due to exogenous ATP10A expression alters the lipid composition at the plasma membrane, which may in turn cause a delay in cell spreading and a change in cell morphology.

TL;DR: Molecular observations help refine models for substrate translocation by P4-ATPases, clarify the relationship between these flippases and human disease, and have fundamental implications for membrane organization and sphingolipid homeostasis.

TL;DR: In this paper, the authors show that the GRAM domain of GRAMD1b possesses distinct but synergistic sites for sensing accessible cholesterol and anionic lipids, including phosphatidylserine (PS) and cholesterol.