Abstract
Cytokinesis in animal cells relies on a centralspindlin complex consisting of male germ cell RacGap (MgcRacGAP) and mitotic kinesin-like protein 1 (MKLP1). Rho GTPases act as molecular switches to regulate the actin cytoskeleton for cytokinesis, of which Rac1 is regulated by MgcRacGAP. In this study, we determined the crystal structure of the GTPase-activating protein (GAP) domain of MgcRacGAP at a resolution of 1.9Å. The conformation of Arg385, which is a key residue for GAP activity, was found to be different from that of previously reported GAP proteins, and MgcRacGAP (residues 348–546) was found to exist as a monomer in solution, according to Stokes radii. We also measured the GAP activity of MgcRacGAP mutants for Rac1.
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