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Generalities

Function

Deubiquitinases or Deubiquitinating enzymes (DUBs) are key enzymes belonging to the vast group of proteases, allowing the degradation of proteins into smaller polypeptides. These enzymes are thus implicated in the protein degradation process. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. This mechanism is called ubiquitination.[1] [1] Following this step, mono or poly-ubiquitin is removed from the protein which has been degraded, by deubiquitinase.

Families

So far, six structural families of DUBs have been discovered. Of these, five belong to the protease family and the last is a family of zinc-dependent metallo-proteases. These enzymes do not play the same role during post-translational modifications : most families allow the removal of one of their substrates, ubiquitin, from the protein (USPs, OTUs, UCHs, Josephins, MINDYs, JAMMs, ULPs). While the Ub cascade family allows ubiquitin to be added to proteins and the UBDs family allow reading and therefore protein-ubiquitin recognition. [1]

Localization

Structure

Biological role

Disease

Structural highlights

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