deubiquitinlaasit

Deubiquitinases, often abbreviated as DUBs, are a class of enzymes that play a crucial role in cellular processes by removing ubiquitin chains from proteins. Ubiquitination, the process of attaching ubiquitin molecules to a target protein, is a versatile post-translational modification that can signal for protein degradation, alter protein function, or regulate protein localization. DUBs act as the opposing force to E3 ubiquitin ligases, which are responsible for attaching ubiquitin.

These enzymes are highly diverse and are classified into several families based on their catalytic mechanisms, including the ubiquitin-specific proteases (USPs), ovarian tumor (OTU) proteases, JAB1/MPN/MOV10 (JAMM) proteases, cysteine-dependent aspartate-specific endopeptidases (CADs), and the proteasome-associated DUBs. Each family possesses a distinct active site that facilitates the cleavage of the isopeptide bond between ubiquitin and the target protein, or between ubiquitin monomers within a chain.

The regulation of protein stability, DNA repair, signal transduction, and immune responses are all influenced by the activity of DUBs. By reversing ubiquitination, DUBs can prevent protein degradation, restore protein function, or modulate signaling pathways. Dysregulation of DUB activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases, making them attractive targets for therapeutic intervention.