Deubiquitinases (DUBs) are a family of proteases whose function is to cleave ubiquitin (Ub) or ubiquitin-like proteins from proproteins or ubiquitin(s) conjugated with target substrate.According to their enzymatic cleavage method, DUBs can be classified into two primary classes: zinc metalloproteases and cysteine proteases. These include Jab1/Mov34/Mpr1 (JAMM) metalloproteases, ovarian tumor proteases, Machado-Joseph disease proteases, ubiquitin-specific proteases (USPs), ubiquitin C-terminal hydrolases (UCHs), and novel DUB family, (MINDY) proteases that contain MIU.
A significant post-translational alteration known as ubiquitination is essential for several crucial biological processes. A coordinated action of the E1, E2, and E3 enzymes results in the attachment of ubiquitin to a substrate protein in this process, and DUBs remove it. DUBs are crucial Ub system regulators because they control a wide range of cellular functions, such as protein sorting, trafficking, and turnover. Alterations in DUB activity have been linked to a wide range of diseases, including cancer. DUBs are fresh options for the creation of drugs that are target-directed.
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