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Molecular and Cellular Biology, September 2002, p. 6498-6508, Vol. 22, No. 18
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.18.6498-6508.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Enzymes of the SUMO Modification Pathway Localize to Filaments of the Nuclear Pore Complex

Hong Zhang,1 Hisato Saitoh,2 and Michael J. Matunis1*

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205,1 Department of Regeneration Medicine, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan2

Received 15 May 2002/ Returned for modification 12 June 2002/ Accepted 13 June 2002

SUMOs are small ubiquitin-related polypeptides that are reversibly conjugated to many nuclear proteins. Although the number of identified substrates has grown rapidly, relatively little is still understood about when, where, and why most proteins are modified by SUMO. Here, we demonstrate that enzymes involved in the SUMO modification and demodification of proteins are components of the nuclear pore complex (NPC). We show that SENP2, a SUMO protease that is able to demodify both SUMO-1 and SUMO-2 or SUMO-3 protein conjugates, localizes to the nucleoplasmic face of the NPC. The unique amino-terminal domain of SENP2 interacts with the FG repeat domain of Nup153, indicating that SENP2 associates with the nucleoplasmic basket of the NPC. We also investigated the localization of the SUMO conjugating enzyme, Ubc9. Using immunogold labeling of isolated nuclear envelopes, we found that Ubc9 localizes to both the cytoplasmic and the nucleoplasmic filaments of the NPC. In vitro binding studies revealed that Ubc9 and SUMO-1-modified RanGAP1 bind synergistically to form a trimeric complex with a component of the cytoplasmic filaments of the NPC, Nup358. Our results indicate that both SUMO modification and demodification of proteins may occur at the NPC and suggest a connection between the SUMO modification pathway and nucleocytoplasmic transport.

* Corresponding author. Mailing address: Johns Hopkins University, Bloomberg School of Public Health, Department of Biochemistry and Molecular Biology, 615 North Wolfe St., Baltimore, MD 21205. Phone: (410) 614-6878. Fax: (410) 955-2926. E-mail: mmatunis{at}jhsph.edu.

Molecular and Cellular Biology, September 2002, p. 6498-6508, Vol. 22, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.18.6498-6508.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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