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SUSP1 antagonizes formation of highly SUMO2/3-conjugated species
Mukhopadhyay, Debaditya Ayaydin, Ferhan Kolli, Nagamalleswari Tan, Shyh-Han Anan, Tadashi Kametaka, Ai Azuma, Yoshiaki Wilkinson, Keith D. Dasso, Mary
Mukhopadhyay, Debaditya
Ayaydin, Ferhan
Kolli, Nagamalleswari
Tan, Shyh-Han
Anan, Tadashi
Kametaka, Ai
Azuma, Yoshiaki
Wilkinson, Keith D.
Dasso, Mary
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Abstract
Small ubiquitin-related modifier (SUMO) processing and deconjugation are mediated by sentrin-specific proteases/ubiquitin-like proteases (SENP/Ulps). We show that SUMO-specific protease 1 (SUSP1), a mammalian SENP/Ulp, localizes within the nucleoplasm. SUSP1 depletion within cell lines expressing enhanced green fluorescent protein (EGFP) fusions to individual SUMO paralogues caused redistribution of EGFP-SUMO2 and -SUMO3, particularly into promyelocytic leukemia (PML) bodies. Further analysis suggested that this change resulted primarily from a deficit of SUMO2/3-deconjugation activity. Under these circumstances, PML bodies became enlarged and increased in number. We did not observe a comparable redistribution of EGFP-SUMO1. We have investigated the specificity of SUSP1 using vinyl sulfone inhibitors and model substrates. We found that SUSP1 has a strong paralogue bias toward SUMO2/3 and that it acts preferentially on substrates containing three or more SUMO2/3 moieties. Together, our findings argue that SUSP1 may play a specialized role in dismantling highly conjugated SUMO2 and -3 species that is critical for PML body maintenance.
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This is the publisher's version, also available electronically from http://jcb.rupress.org/content/174/7/939
Date
2006-09-21
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The Rockefeller University Press
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AzumaY_2006.pdf
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Mukhopadhyay, Debaditya et al. (2006). "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species." Journal of Cell Biology, 174(7):939-949. http://www.dx.doi.org/10.1083/jcb.200510103