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Published 25 September 2006. doi:10.1083/jcb.200510103
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 7, 939-949
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Article

SUSP1 antagonizes formation of highly SUMO2/3-conjugated species



Debaditya Mukhopadhyay1, Ferhan Ayaydin1, Nagamalleswari Kolli2, Shyh-Han Tan1, Tadashi Anan1, Ai Kametaka1, Yoshiaki Azuma1,3, Keith D. Wilkinson2, and Mary Dasso1

1 Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892
2 Department of Biochemistry, Emory University, Atlanta, GA 30322
3 Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045

Correspondence to Mary Dasso: mdasso{at}helix.nih.gov

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.

F. Ayaydin, N. Kolli, and S.-H. Tan contributed equally to this paper.

F. Ayaydin's present address is Hungarian Academy of Sciences, H-6701 Szeged, Hungary.

S.-H. Tan's present address is Department of Cancer Biology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107.

T. Anan's present address is Department of Pediatrics, Kumamoto University School of Medicine, Kumamoto 860-0811, Japan.

Abbreviations used in this paper: BLM, Bloom's antigen; PML, promyelocytic leukemia protein; RanGAP1, Ran GTPase-activating protein 1; RFP, red fluorescent protein; SENP, sentrin-specific protease; SUMO, small ubiquitin-related modifier; SUSP1, SUMO-specific protease 1; Ulp, ubiquitin-like protease; VS, vinyl sulfone.


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