O-GlcNAc inhibits interaction between Sp1 and sterol regulatory element binding protein 2.
O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine on the serine and threonine residues of nucleocytoplasmic proteins, is a novel protein modification that is ubiquitous among eukaryotes and implicated in cell regulation. Recent evidence indicates that O-GlcNAc regulates protein-protein interactions. Here we provide evidence that O-GlcNAc interrupts a known interaction between Sp1 and sterol regulatory element binding protein 2 (SREBP2), thereby inhibiting expression of the gene encoding acetyl-CoA synthetase 1, which is involved in lipid synthesis. This study suggests a novel mechanism in which lipid biosynthesis may be regulated by O-GlcNAc.
Korea University, Anam-dong, Seongbuk-gu, Seoul, Republic of Korea.
Kihong
K
Lim
Hyo-Ihl
HI
Chang
D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D003066:Coenzyme A Ligases / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008055:Lipids / Q000096:biosynthesis* / Q000235:genetics; D051379:Mice; D016329:Sp1 Transcription Factor / Q000037:antagonists & inhibitors* / Q000378:metabolism; D051782:Sterol Regulatory Element Binding Protein 2 / Q000037:antagonists & inhibitors* / Q000378:metabolism; D014158:Transcription, Genetic
D008055:Lipids; D016329:Sp1 Transcription Factor; D051782:Sterol Regulatory Element Binding Protein 2; D003066:Coenzyme A Ligases; C101958:acetate-CoA ligase (ADP-forming); D000117:Acetylglucosamine