Triggered Assembly of Functional Protein Microdomains in the Cytosol

摘要

The ability to precisely control or alter cellular machinery remains challenging. If it were possible to alter cytosolic processes inside living cells, it would prove to be a great tool in understanding trafficking and complex signaling pathways in specific diseases. To address this issue, we report that Elastin-like polypeptides (ELPs), which belong to a class of environmentally responsive protein polymers, have the ability to not only assemble but also to control specific cytosolic machinery inside living cells. To test this hypothesis, ELP fusion proteins were cloned in mammalian vector and transfected in mammalian cells. At low temperatures, ELP fusion proteins remain soluble. However, at physiological temperatures, ELPs phase separate which causes the fusion protein to assemble into microdomains. This assembly prevents the functional protein domain’s inherent ability to carry out signaling pathways.