The ubiquitin proteasome pathway, conserved from yeast to mammals, is required for the targeted degradation of most short-lived proteins in the eukaryotic cell. Targets include cell cycle regulatory proteins, whose destruction is vital for controlled cell division, as well as proteins unable to fold properly within the endoplasmic reticulum. Ubiquitination, a post-translational modification, involves the sequential action of ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The reaction catalyzed by each enzyme transfers a covalent bond with ubiquitin from one enzyme to the next and finally to a target protein.

 

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