Thanks André!

Finally, big congrats to all authors, including collaborators from the @pdc-lab.bsky.social, and thanks to @snsf.ch and @erc.europa.eu for funding this research line in my lab. Looking forward to your comments and feedback! (7/7)

Finally, @danialv.bsky.social used CG simulations to show that VPS13A can deliver lipids to an acceptor membrane that is bound at the C-terminal of VPS13A, and that XKR1 is proximal, but not continuous, to the delivery site. (6/7)

But how does VPS13A contact the lipid bilayer? Using a combination of coarse-grained (CG) MD simulation and in vitro flotation assay, we show that a disordered ATG2_C domain located in the C-terminal part of VPS13A is required for membrane binding. (5/7)

The plasma membrane scramblase XKR1 directly interacts with the PH domain of VPS13A. All-atom MD simulations show that this interaction promotes a conformational change in XKR1 which exposes a hydrophilic groove, that acts as the scrambling region (4/7)

The cryo-EM data reveal that the VAB domain of VPS13A can adapt distinct conformations. These are likely to modulate the lipid transfer ability of VPS13A, and this mechanism is probably conserved in similar BLTPs. (3/7)

The first step: at Yale, Bodan solved at near-atomic resolution the structure a prototypical BLTP, VSP13A, in complex with Calmodulin (CaM) and a plasma membrane scramblase, XKR1, demonstrating their physical interaction. (2/7)