High-throughput CGMD simulations enable proteome-wide identification of lipid scramblases in yeast

Presenting author: Cristian Rocha Roa

Fribourg University, Fribourg, Switzerland, Department of Biology, Chemin du Musée 10, 1700 Fribourg [CH], cristian.rocharoa@unifr.ch

Author(s):
Cristian Rocha Roa, Stefano Vanni

Membrane proteins constitute nearly a quarter of the proteins encoded in most organisms, representing approximately 50% of the cell membrane mass. Therefore, lipid-protein interactions are crucial for many cellular processes, and lipid transport between organelles is essential for cellular homeostasis. It has been demonstrated that lipid transport proteins team-up with lipid scramblase proteins. This protein-protein complex is proposed to be required for processes such as membrane expansion, e.g. autophagosome biogenesis. Using coarse-grained molecular dynamics simulations of predicted structures from AlphaFold2 for the yeast S. cerevisiae, we have identified several previously unknown putative lipid scramblase proteins. As a consequence of the presence of these new putative scramblases, our results suggest that cell membranes are more dynamic than previously thought. They provide an initial framework for understanding how the cell regulates its lipid membrane and open the door to new interpretations of previous gaps in lipid-mediated processes.

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