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Prepublished online as a Blood First Edition Paper on July 10, 2003; DOI 10.1182/blood-2002-12-3816. This Article Full Text (PDF) All Versions of this Article: 2002-12-3816v1 102/9/3311    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Ungureanu, D. Articles by Silvennoinen, O. Search for Related Content PubMed PubMed Citation Articles by Ungureanu, D. Articles by Silvennoinen, O. Social Bookmarking                   What's this? Submitted December 17, 2002 Accepted June 25, 2003 PIAS proteins promote SUMO-1 conjugation to STAT1 Daniela Ungureanu, Sari Vanhatupa, Noora Kotaja, Jie Yang, Saara Aittomaki, Olli A Janne, Jorma J Palvimo, and Olli Silvennoinen* Department of Molecular Immunology, Institute of Medical Technology, Tampere, Finland; Department of Clinical Microbiology, Tampere University Hospital, Tampere, Finland Biomedicum Helsinki, Helsinki, Finland Department of Clinical Chemistry, Biomedicum Helsinki, Helsinki, Finland Institute of Biotechnology, University of Helsinki, Helsinki, Finland Helsinki University Central Hospital, Helsinki, Finland * Corresponding author; email: olli.silvennoinen{at}uta.fi. Signal Transducer and Activator of Transcription 1 (STAT1) is a critical mediator of interferon- (IFN-)-induced transcription, that is regulated through posttranslational modifications and through transacting proteins such as Protein Inhibitor of Activated STAT1 (PIAS1). PIAS proteins have been shown to function as E3 SUMO ligases, and sumoylation has been identified as a modulatory mechanism for several transcription factors. Here we show that STAT1 is subject to SUMO-1 modification, and sumoylation occurs in vivo and in vitro at a single, evolutionary conserved amino acid residue Lys703. Members of the PIAS family of proteins were found to strongly stimulate sumoylation of STAT1. Furthermore, activation of STAT1 by IFN- or pervanadate induced SUMO-1 conjugation. Mutation of Lys703 in STAT1 resulted in increased IFN--mediated transactivation, suggesting a negative regulatory function for sumoylation. These results indicate that STAT1 is covalently modified by SUMO-1 in cytokine signaling, and that PIAS proteins promote SUMO-1 conjugation to STAT1. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Dabir, A. Kluge, and A. 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