title: AIMP1 negatively regulates adipogenesis by inhibiting PPARγ.
abstract: Adipogenesis is known to be controlled by the concerted actions of transcription factors and co-regulators. However, little is known about the mechanism of regulation of the transcription factors that control adipogenesis. In addition, the adipogenic roles of translational factors remain unclear. Here, we show that aminoacyl tRNA synthetase-interacting multifunctional protein 1 (AIMP1, also known as p43), an auxiliary factor that is associated with a macromolecular tRNA synthetase complex, negatively regulates adipogenesis through a direct interaction with the DNA-binding domain of peroxisome proliferator-activated receptor γ (PPARγ). We found that AIMP1 expression increases during adipocyte differentiation. Adipogenesis is augmented in AIMP1-deficient cells, as compared with control cells. AIMP1 exhibits high affinity for active PPARγ and interacts with the DNA-binding domain of PPARγ, thereby inhibiting its transcriptional activity. Thus, AIMP1 appears to function as a novel inhibitor of PPARγ that regulates adipocyte differentiation by preventing the transcriptional activation of PPARγ.
authors.affiliation: Medicinal Bioconvergence Research Center, Seoul National University, Seoul 151-742, South Korea.
authors.forename: Jong Hyun
authors.initials: JH
authors.lastname: Kim
authors.affiliation: College of Pharmacy, Seoul National University, Seoul 151-742, South Korea.
authors.forename: Jung Ho
authors.initials: JH
authors.lastname: Lee
authors.affiliation: Medicinal Bioconvergence Research Center, Seoul National University, Seoul 151-742, South Korea.
authors.forename: Min Chul
authors.initials: MC
authors.lastname: Park
authors.affiliation: Medicinal Bioconvergence Research Center, Seoul National University, Seoul 151-742, South Korea.
authors.forename: Ina
authors.initials: I
authors.lastname: Yoon
authors.affiliation: Medicinal Bioconvergence Research Center, Seoul National University, Seoul 151-742, South Korea.
authors.forename: Kibom
authors.initials: K
authors.lastname: Kim
authors.affiliation: Department of Integrated OMICS for Biomedical Science, Yonsei University, Seoul 120-749, South Korea.
authors.forename: Minji
authors.initials: M
authors.lastname: Lee
authors.affiliation: National Creative Research Initiatives Center for Nuclear Receptor Signals, School of Biological Sciences and Technology, Chonnam National University, Gwangju 500-757, South Korea.
authors.forename: Hueng-Sik
authors.initials: HS
authors.lastname: Choi
authors.affiliation: Department of Integrated OMICS for Biomedical Science, Yonsei University, Seoul 120-749, South Korea College of Pharmacy, Yonsei University, Incheon 406-840, South Korea jhan74@yonsei.ac.kr sungkim@snu.ac.kr.
authors.forename: Jung Min
authors.initials: JM
authors.lastname: Han
authors.affiliation: Medicinal Bioconvergence Research Center, Seoul National University, Seoul 151-742, South Korea College of Pharmacy, Seoul National University, Seoul 151-742, South Korea Department of Molecular Medicine and Biopharmaceutical Sciences, Seoul National University, Seoul 151-742, South Korea jhan74@yonsei.ac.kr sungkim@snu.ac.kr.
authors.forename: Sunghoon
authors.initials: S
authors.lastname: Kim
mesh_terms: D016475:3T3 Cells; D017667:Adipocytes / Q000502:physiology*; D050156:Adipogenesis / Q000235:genetics*; D000818:Animals; D000831:Animals, Newborn; D016207:Cytokines / Q000235:genetics / Q000378:metabolism*; D004622:Embryo, Mammalian; D005786:Gene Expression Regulation; D006801:Humans; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D047495:PPAR gamma / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic / Q000235:genetics
chemical_list: D016207:Cytokines; D009363:Neoplasm Proteins; D047495:PPAR gamma; D016601:RNA-Binding Proteins; C077219:small inducible cytokine subfamily E, member 1
keywords: AIMP1; Adipogenesis; PPARγ; tRNA synthetase