O-GlcNAc modification of Sp1 inhibits the functional interaction between Sp1 and Oct1.
Sp1 is a ubiquitous transcription factor that is modified by multiple O-linked N-acetylglucosamines (O-GlcNAc). Previously, O-GlcNAcylation of a specific site of Sp1 was shown to inhibit Sp1 transcriptional activity. Yet, how O-GlcNAc on other modification sites affects Sp1 function and how O-GlcNAcylation of Sp1 affects the transcriptional regulation of a target gene remains unknown. Here we show that O-GlcNAc within the second serine/threonine-rich region of Sp1 interrupts a known interaction between Sp1 and Oct1, and inhibits the cooperative activation of the U2 snRNA gene by Sp1 and Oct1.
Lim
Kihong
K
School of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.
Chang
Hyo-Ihl
HI
D000117:Acetylglucosamine / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D027702:Organic Cation Transporter 1 / Q000235:genetics / Q000378:metabolism*; D011401:Promoter Regions, Genetic / Q000235:genetics; D011485:Protein Binding; D012342:RNA, Small Nuclear / Q000235:genetics; D012694:Serine / Q000378:metabolism; D016329:Sp1 Transcription Factor / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism; D014158:Transcription, Genetic / Q000235:genetics
D027702:Organic Cation Transporter 1; D012342:RNA, Small Nuclear; D016329:Sp1 Transcription Factor; D013912:Threonine; D012694:Serine; D000117:Acetylglucosamine