Our cells function in the continuous mode of producing and degrading proteins, keeping the balance between these two processes to maintain a healthy cellular function. However, sometimes the produced proteins might be defective, accumulating and causing pathological effects. This is one of the examples when hijacking the naturally occurring process of protein degradation becomes highly useful for rescuing the cells.
When the time comes, in the majority of cases ubiquitin-proteasome system (UPS) takes over proteins. The sequence of enzymatic reactions leads to marking doomed proteins by the ubiquitin chain, which is done by E3 ubiquitin ligase. This causes the signaling cascade and, consequently, proteasomal recycling of proteins into the new building blocks.
Scientists figured out a way to force E3 ubiquitin ligase to get in proximity with any protein of interest so that the UPS can be involved in the targeted protein degradation -- by applying "molecular glues" or proteolysis-targeting chimeras, or PROTACs, the two most popular strategies to go about protein degradation.
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