Anillin-related Mid1 as an adaptive and multimodal contractile ring anchoring protein: A simulation study.

Aaron R Hall, Yeol Kyo Choi, Wonpil Im, Dimitrios Vavylonis

Structure (London, England : 1993) 2024 Feb 01

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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. Copyright © 2023 Elsevier Ltd. All rights reserved.

Citation

Aaron R Hall, Yeol Kyo Choi, Wonpil Im, Dimitrios Vavylonis. Anillin-related Mid1 as an adaptive and multimodal contractile ring anchoring protein: A simulation study. Structure (London, England : 1993). 2024 Feb 01;32(2):242-252.e2