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Function and regulation of SUMO proteases

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 13, Issue 12, Pages 755-766

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3478

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Funding

  1. US National Institutes of Health (NIH) [GM046904, GM053756]
  2. NIH National Research Service Award (NRSA) postdoctoral fellowship [F32 GM097794]
  3. National Science Foundation (NSF) predoctoral fellowship

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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.

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