{Reference Type}: Journal Article
{Title}: Anillin-related Mid1 as an adaptive and multimodal contractile ring anchoring protein: A simulation study.
{Author}: Hall AR;Choi YK;Im W;Vavylonis D;
{Journal}: Structure
{Volume}: 32
{Issue}: 2
{Year}: 2024 Feb 1
{Factor}: 5.871
{DOI}: 10.1016/j.str.2023.11.010
{Abstract}: Cytokinesis of animal and fungi cells depends crucially on the anillin scaffold proteins. Fission yeast anillin-related Mid1 anchors cytokinetic ring precursor nodes to the membrane. However, it is unclear if both of its Pleckstrin Homology (PH) and C2 C-terminal domains bind to the membrane as monomers or dimers, and if one domain plays a dominant role. We studied Mid1 membrane binding with all-atom molecular dynamics near a membrane with yeast-like lipid composition. In simulations with the full C terminal region started away from the membrane, Mid1 binds through the disordered L3 loop of C2 in a vertical orientation, with the PH away from the membrane. However, a configuration with both C2 and PH initially bound to the membrane remains associated with the membrane. Simulations of C2-PH dimers show extensive asymmetric membrane contacts. These multiple modes of binding may reflect Mid1's multiple interactions with membranes, node proteins, and ability to sustain mechanical forces.