Associate Professor at UConn studying Toxoplasma gondii, myosin motors, actin organization and vesicle trafficking. Twin Mom. she|her
Aoife Heaslip
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This creates a compelling model where multi-headed MyoF assemblies generate force collectively to reorganize actin networks rather than simply transporting vesicles.
Full-length MyoF behaves differently - Single molecules can move on bundled or parasite actin filaments. The explanation is oligomerization mediated by the WD40 β-propeller tail domain.
Toxoplasma infects ~1/3 of the global population. To survive, the parasite uses actin filaments to precisely organize and transport cargo inside the cell. Prior work showed MyoF is essential for vesicle transport and actin dynamics but HOW it worked biophysically was unclear.
So, MyoF oligomers remodel actin architecture. This is important because apicomplexan actin systems are highly divergent from canonical eukaryotic models. The study helps explain how parasites evolved specialized solutions for intracellular organization.
MyoF contains a distinctive WD40 β-propeller domain found only in Apicomplexa and closely related species. Motors lacking the WD40 tail can bind/translocate actin, but cannot "walk" along actin as a single molecule – a characteristic typically found in cargo transport motors.
