Targeted protein degradation has emerged as a transformative approach in drug discovery . Protein degradation offers significant advantages over protein inhibition: long-lasting therapeutic effects upon removal of the target protein, lower drug concentrations for achieving therapeutic activity, and a wider array of protein targets. Unlike inhibition, which is limited to the presence of a specific functional domain or active site in a protein, degradation has no such constraints -expanding the druggable proteome. One of the most promising class of molecules for targeted protein degradation are proteolysis-targeting chimeras (PROTACs) . These catalytic, heterobifunctional small molecules simultaneously bind a protein of interest (POI) and an E3 ligase . This binding induces a proximitydependant ubiquitination of the POI by the E3 ligase, marking it for degradation by the ubiquitinproteasome system . Thereby, hijacking a natural cellular process responsible for maintaining protein homeostasis to enable targeted protein degradation.