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Caption N-terminal domain A/B domain : ligand-independent domain AF1: Activation F unction 1

Structural Organization of PPARγ. Caption N-terminal domain A/B domain : ligand-independent domain AF1: Activation F unction 1 DBD: DNA B inding D omain LBD: L igand B inding Domain: ligand - dependent domain AF2: Activation Function 2 C-terminal domain. Sumoylation.

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Caption N-terminal domain A/B domain : ligand-independent domain AF1: Activation F unction 1

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  1. StructuralOrganization of PPARγ Caption N-terminaldomain A/B domain: ligand-independentdomain AF1: ActivationFunction 1 DBD: DNA Binding Domain LBD: LigandBinding Domain: ligand-dependentdomain AF2: ActivationFunction 2 C-terminaldomain Sumoylation Phosphorylation

  2. StructuralOrganization of PPARγ-1 and PPARγ-2 PPARγ-1 PPARγ-2 PPARγ-1 and PPARγ-2 areisoforms of PPARγ. PPARγ and PPARγ-1 arestructurallyidentical, though PPARγ-2 has a longer N-terminal domain (30-residue extension of aminoacids).

  3. a) Phosphorylation of PPARγ-2 Thephosphorylation of PPARγ-2 takesplace on S112 (serine 112 site) on the AF1 region. The phosphorylationactivatesthereceptor and results in theadipogenicgeneprogram. b) Phosphorylation and Sumoylation of PPARγ-2 Phosphorylation of S112 togetherwithsumoylation of K107 of PPARγ-2 occurs on the AF1 region.Thisarrayinhibitstheactivity of thereceptor and results in a reducedadipogenicgeneprogram. c) Sumoylation of PPARγ-2 Thesumoylation of K107 of PPARγ-2 occurs on the AF2 region. Itisimportantforligand-dependentrepression of theinflammatorygeneprogram.

  4. c) Ubiquitination of PPARγ-2 Ubi K107 sumoylationistosomeextentlinkedto S112 phosphorylation. Sumoylation of transcriptionalregulatorsmostlycorrelateswiththeinhibition of transcription. Itisassumedthatphosphorylationcanindicateinhibitionorstimulation of transcriptionalactivity, depending on thecellularbackground and kinasesinvolved.

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