Light Triggered Molecular Motor, Massachusetts Institute of Technology (MIT) and Collaborators Reveal

Barbara Imperiali and a team from the Massachusetts Institute of Technology (Cambridge, USA), the University of Virginia (Charlottesville, USA), and the National Institutes of Health (USA) have now provided the motor protein myosin with an "on switch" that is activated by light. As the scientists report in the journal Angewandte Chemie, this should make it possible to follow cellular processes that involve myosin in real time. In order for our muscles to contract, two types of fibrous proteins, myosin and actin, must interact. Driven by splitting of the cellular fuel adenosine triphosphate (ATP), "buttons" on the myosin molecules attach, allowing the myosin to dangle off of the actin filaments. In non-muscular cells, myosin ensures that the cell constricts itself in the division process. Myosin consists of several different protein chains. The activity of non-muscular myosin is regulated through its regulatory light chain. As soon as a phosphate group binds to a specific site (Ser19) of the light chain (phosphorylation), myosin become active. The activity can be amplified through binding of a second phosphate group at a neighboring site (Thr18).

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