title: Role of TG-interacting factor (Tgif) in lipid metabolism.
abstract: TG interacting factors (Tgifs) 1 and 2 are members of the TALE (three-amino-acid loop extension) superfamily of homeodomain proteins. These two proteins bind to the same DNA sequence and share a conserved C-terminal repression domain. Mutations in TGIF1 have been linked to holoprosencephaly, which is a human genetic disease that affects craniofacial development. As these proteins can interact with the ligand binding domain of retinoid X receptor α, a common heterodimeric partner of several nuclear receptors [e.g., liver X receptors (LXRs) and peroxisome proliferator-activated receptors (PPARs)], Tgif1 and Tgif2 might repress other transcriptional pathways activated by lipids. In line with this, Tgif1 interacts with LXRα and Tgif1 null mice have increased expression of the two Lxrα target genes apolipoproteins (Apo) c2 and a4. Also, we have recently identified Tgif1 to function as a transcriptional repressor of the cholesterol esterifying enzyme acyl-coenzyme A:cholesterol acyltransferase 2 (gene name SOAT2). As no studies yet have shown involvement of Tgif2 in the lipid metabolism, this review will focus on the role of Tgif1 in lipid and cholesterol metabolism. This article is part of a Special Issue entitled: Linking transcription to physiology in lipodomics.
authors.affiliation: Division of Clinical Chemistry, Department of Laboratory Medicine, Centre for Nutrition and Toxicology, NOVUM, Karolinska Institutet at Karolinska University Hospital Huddinge, Sweden; Molecular Nutrition Unit, Department of Biosciences and Nutrition, Centre for Nutrition and Toxicology, NOVUM, Karolinska Institutet at Karolinska University Hospital Huddinge, Sweden.
authors.forename: Camilla
authors.initials: C
authors.lastname: Pramfalk
authors.affiliation: Molecular Nutrition Unit, Department of Biosciences and Nutrition, Centre for Nutrition and Toxicology, NOVUM, Karolinska Institutet at Karolinska University Hospital Huddinge, Sweden; Metabolism Unit, Department of Endocrinology, Metabolism and Diabetes, and Department of Medicine, Karolinska Institutet at Karolinska University Hospital, Huddinge, S-141 86 Stockholm, Sweden.
authors.forename: Mats
authors.initials: M
authors.lastname: Eriksson
authors.affiliation: Division of Clinical Chemistry, Department of Laboratory Medicine, Centre for Nutrition and Toxicology, NOVUM, Karolinska Institutet at Karolinska University Hospital Huddinge, Sweden; Molecular Nutrition Unit, Department of Biosciences and Nutrition, Centre for Nutrition and Toxicology, NOVUM, Karolinska Institutet at Karolinska University Hospital Huddinge, Sweden. Electronic address: paolo.parini@ki.se.
authors.forename: Paolo
authors.initials: P
authors.lastname: Parini
mesh_terms: D000818:Animals; D002784:Cholesterol / Q000378:metabolism; D005801:Genes, Homeobox; D018398:Homeodomain Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D050356:Lipid Metabolism / Q000502:physiology*; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D018398:Homeodomain Proteins; D012097:Repressor Proteins; C505201:TG-interacting factor 2, mouse; C097504:TGIF1 protein, human; C414585:TGIF2 protein, human; C490797:Tgif1 protein, mouse; D002784:Cholesterol
keywords: Lipid metabolism; RXRα; SOAT2; Tgif1; Tgif2