Ubiquitin recruiting chimera: more than just a PROTAC
Grigoreva T.A. Novikova D.S. Melino G. Barlev N.A. Tribulovich V.G.
December 2024BioMed Central Ltd
Biology Direct
2024#19Issue 1
Ubiquitinylation of protein substrates results in various but distinct biological consequences, among which ubiquitin-mediated degradation is most well studied for its therapeutic application. Accordingly, artificially targeted ubiquitin-dependent degradation of various proteins has evolved into the therapeutically relevant PROTAC technology. This tethered ubiquitinylation of various targets coupled with a broad assortment of modifying E3 ubiquitin ligases has been made possible by rational design of bi-specific chimeric molecules that bring these proteins in proximity. However, forced ubiquitinylation inflicted by the binary warheads of a chimeric PROTAC molecule should not necessarily result in protein degradation but can be used to modulate other cellular functions. In this respect it should be noted that the ubiquitinylation of a diverse set of proteins is known to control their transport, transcriptional activity, and protein-protein interactions. This review provides examples of potential PROTAC usage based on non-degradable ubiquitinylation.
PROTAC , Protein degradation , Ubiquitin
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Laboratory of Molecular Pharmacology, St. Petersburg State Institute of Technology (Technical University), St. Petersburg, 190013, Russian Federation
Department of Experimental Medicine, University of Rome Tor Vergata, Rome, 00133, Italy
Institute of Cytology RAS, Saint-Petersburg, 194064, Russian Federation
Department of Biomedical Studies, School of Medicine, Nazarbayev University, Astana, 010000, Kazakhstan
Laboratory of Molecular Pharmacology
Department of Experimental Medicine
Institute of Cytology RAS
Department of Biomedical Studies
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