Selected article for: "intracellular localization and nuclear localization"

Author: Wilson, Van G.
Title: Sumoylation at the Host-Pathogen Interface
  • Document date: 2012_4_5
  • ID: 1awau7hm_2
    Snippet: Lastly, the sumoylation state of target proteins is not static, but instead reflects a dynamic equilibrium between the forward process of SUMO addition and its removal by cellular desumoylating enzymes known as SENPs [34] . The mammalian SUMO proteases differ greatly in their sequences and are related primarily in the conserved region critical for cysteine protease catalytic activity. Furthermore, individual proteases have been shown to differ in.....
    Document: Lastly, the sumoylation state of target proteins is not static, but instead reflects a dynamic equilibrium between the forward process of SUMO addition and its removal by cellular desumoylating enzymes known as SENPs [34] . The mammalian SUMO proteases differ greatly in their sequences and are related primarily in the conserved region critical for cysteine protease catalytic activity. Furthermore, individual proteases have been shown to differ in intracellular localization with both nuclear [35, 36] and cytoplasmic [37] [38] [39] species observed. The existence of multiple mammalian desumoylating enzymes, along with the demonstrated differences in intracellular distribution, suggests that desumoylation is likely to be a complex process that contributes to the regulation of activity of SUMO substrates.

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