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      Function and Regulation of SUMO Proteases

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          Abstract

          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 performed 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 for the study of these enzymes.

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          Author and article information

          Journal
          100962782
          22271
          Nat Rev Mol Cell Biol
          Nat. Rev. Mol. Cell Biol.
          Nature reviews. Molecular cell biology
          1471-0072
          1471-0080
          23 May 2013
          December 2012
          01 June 2013
          : 13
          : 12
          : 755-766
          Affiliations
          Department of Molecular Biophysics and Biochemistry Yale University 266 Whitney Avenue New Haven, CT 06520
          Author notes
          Contact: mark.hochstrasser@ 123456yale.edu Phone: 001-203-432-5101 Fax: 001-203-432-6507
          Article
          PMC3668692 PMC3668692 3668692 nihpa476209
          10.1038/nrm3478
          3668692
          23175280
          1e70cc39-4095-48e7-94b5-f88dda7d79ee
          History
          Funding
          Funded by: National Institute of General Medical Sciences : NIGMS
          Award ID: R37 GM046904 || GM
          Funded by: National Institute of General Medical Sciences : NIGMS
          Award ID: R01 GM053756 || GM
          Funded by: National Institute of General Medical Sciences : NIGMS
          Award ID: F32 GM097794 || GM
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