کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1934953 | 1050653 | 2008 | 6 صفحه PDF | دانلود رایگان |
Sumoylation is reversibly regulated by SUMO-specific proteases. We characterized a nucleolar SUMO-specific protease, SMT3IP1, which has a preference for SUMO-2/3. To elucidate SMT3IP1 function, we screened for its interacting proteins that may be its substrates or regulate its activity. By using yeast two-hybrid screening, we identified nucleophosmin (NPM) as an SMT3IP1-binding partner. SMT3IP1 could preferentially remove SUMO-2 from sumoylated NPM. A catalytically inactive SMT3IP1 mutant increased intracellular accumulation of SUMO-2-modified NPM in a dominant-negative manner. Sumoylation of cytoplasmic mutated NPM was markedly elevated in an ARF-dependent manner. Despite the divergence in their localization, ectopic expression of SMT3IP1 could desumoylate a SUMO-2-modified NPM mutant. Additionally, genotoxic drugs caused the dissociation of NPM from nucleolar co-localization with SMT3IP1, but did not affect desumoylation of NPM by SMT3IP1. Our findings suggest that SMT3IP1-mediated desumoylation might control NPM physiological functions at both the nucleolus and other subcellular compartments.
Journal: Biochemical and Biophysical Research Communications - Volume 374, Issue 2, 19 September 2008, Pages 382–387