Deubiquitinating enzymes (DUBs) that specifically disassemble ubiquitin chains or regulate ubiquitin homeostasis reside as a central component in ubiquitin signaling. Over 100 genes potentially coding for DUBs could be identified in the human genome. DUBs are classified into five distinct families. Four families are identified as cysteine proteases, including ubiquitin C-terminal hydrolases (UCH), the ubiquitin-specific proteases (USP/UBPs), Otubain domain ubiquitin-binding proteins (OTU), Machado-Joseph domain (Josephin domain)-containing (MJD) proteases. The fifth family of DUBs is Jab1/Pab1/MPN domain-containing (JAMM) protease, which belongs to metalloprotease family.
General cellular role of DUBs
- Deubiquitination of substrate proteins: Editing the ubiquitination process if any substrate is wrongly labeled thus, can help in exchanging one type of ubiquitin signal to another.
- Rescue of substrate from degradation: DUBs can rescue proteins from degradation by cleaving degradative signals.
- Removal of functional signal: DUBs control cellular signaling process by removing non degradative signals.
- Recycling of ubiquitin: DUBs play important role in preventing proteasomal degradation of ubiquitin along with substrate and maintain overall free ubiquitin pool.
- Free chain processing: DUBs can cleave free poly ubiquitin chains and recycle the ubiquitin into the system.
- Ubiquitin precursor processing: Ubiquitin is formed as a fused precursor protein consisting of multiple copies of ubiquitin, and DUBs help in generation of free functional ubiquitin from these precursors.
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