Function and Regulation of SUMO Proteases

By Christopher M Hickey, Nicole R Wilson, M. Hochstrasser. Nature reviews. Molecular cell biology, 2012

627 citations recorded by the source corpus.

Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins is highly dynamic, and both SUMO–protein conjugation and cleavage can be regulated. Protein desumoylation is carried out by SUMO proteases, which control cellular mechanisms ranging from transcription and cell division to ribosome biogenesis. Recent advances include the discovery of two novel classes of SUMO proteases, insights regarding SUMO protease specificity, and revelations of previously unappreciated SUMO protease functions in several key cellular pathways. These developments, together with new connections between SUMO proteases and the recently discovered SUMO-targeted ubiquitin ligases (STUbLs), make this an exciting period to study these enzymes.

Subfields: Molecular Biology, Oncology, Parasitology

View Paper: https://www.semanticscholar.org/paper/08171bc201af637a850d228fded3bd596adbcda7

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In Molecular Biology

1. F. Melchior
2. Annette Flotho
3. A. Hata
4. Ye-Guang Chen

In Oncology

1. F. Melchior
2. Ye-Guang Chen
3. A. Hata

In Parasitology

1. F. Melchior
2. Annette Flotho

Citations in the corpus

• Sumoylation: a regulatory protein modification in health and disease. (2013, background): “Dedicated SUMO-specific proteases reverse the modification by stimulating hydrolysis of the isopeptide bond (10, 11).”