monoubiquitinated protein deubiquitination

Definition

Target type: biologicalprocess

The removal of the ubiquitin group from a monoubiquitinated protein. [GOC:bf]

Monoubiquitinated protein deubiquitination is a crucial cellular process that involves the removal of a single ubiquitin moiety from a target protein. This process is catalyzed by deubiquitinating enzymes (DUBs), a diverse family of proteases that specifically recognize and cleave the isopeptide bond between ubiquitin and its substrate.

The process typically begins with the recruitment of a DUB to a monoubiquitinated protein. DUBs often possess specific substrate binding domains that allow them to interact with the target protein, as well as with ubiquitin itself. Upon binding, the DUB utilizes its catalytic domain to hydrolyze the isopeptide bond, releasing the ubiquitin moiety from the substrate.

This process is tightly regulated and plays a vital role in various cellular processes, including:

* **Signal transduction:** Ubiquitination and deubiquitination act as molecular switches, regulating the activity of signaling proteins and modulating cellular responses.
* **Protein trafficking:** Deubiquitination is involved in the sorting and transport of proteins within the cell, facilitating their proper localization and function.
* **DNA repair:** Monoubiquitination and deubiquitination are essential for the recruitment and activation of DNA repair machinery, ensuring the integrity of the genome.
* **Cell cycle control:** Deubiquitination regulates the activity of key cell cycle regulators, ensuring proper progression through the cell cycle.

Dysregulation of deubiquitination has been implicated in various human diseases, including cancer, neurodegenerative disorders, and immune system dysfunction. Therefore, understanding the mechanisms of monoubiquitinated protein deubiquitination is crucial for developing novel therapeutic strategies.'
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Proteins (7)

Compounds (19)