Stat1 depends on transcriptional synergy with Sp1

Dwight C. Look, Mark B. Pelletier, Rose M. Tidwell, William T. Roswit, Michael J. Holtzman

Research output: Contribution to journalArticlepeer-review

235 Scopus citations

Abstract

STAT (signal transducer and activator of transcription) proteins combine with cytokine receptors and receptor-associated kinases in distinct protein/protein interactions that are critical for STAT-dependent signal transduction events, but the nature of any subsequent STAT interactions with DNA-binding proteins in the nucleus is less certain. Based on assays of DNA/protein binding and activity of transfected reporter plasmids, we determined that occupation of contiguous DNA-binding sites for Stat1 (the first member of the STAT family) and the transcriptional activator Sp1 are both required for full activation of the intercellular adhesion molecule-1 gene by interferon-γ. Thus, Stat1 binding to DNA cannot by itself be equated with biologic actions of Stat1. In co-immunoprecipitation experiments, we also obtained evidence of direct and selective Stat1/Sp1 interaction (in primary culture cells without overexpression), further indicating that Stat1/Sp1 synergy confers an element of specificity in the pathway leading to cytokine-activated transcription and cytokine-dependent immunity and inflammation.

Original languageEnglish
Pages (from-to)30264-30267
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number51
DOIs
StatePublished - Dec 22 1995

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