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. Author manuscript; available in PMC: 2010 Sep 25.
Published in final edited form as: Nature. 2010 Mar 3;464(7288):619–623. doi: 10.1038/nature08816

Figure 3. Zfp423 amplifies the pro-adipogenic actions of BMP proteins through its SMAD protein interaction domain.

Figure 3

(a) Schematic illustrating the protein domains and zinc-finger (ZF) motifs of full length Zfp423 and Zfp423 lacking the SMAD binding domain (Zfp423 ΔSBD). ZF 14-20 serves as the well-characterized SMAD interaction domain. (b) Western blot of ectopic full length Zfp423 or Zfp423 ΔSBD protein expression in NIH 3T3 cells. Tubulin protein levels serve as a loading control. (c) PPARγ2 mRNA levels in undifferentiated cells expressing Zfp423 or Zfp423 ΔSBD. (d) Expression of adipocyte selective mRNAs in cultures following differentiation with DMI and Rosiglitazone and ORO staining of differentiated cultures. (e) PPARγ2 mRNA levels in undifferentiated NIH 3T3 cells expressing a control vector or full length Zfp423 following 48 hours of incubation with increasing doses of BMP4. (f) PPARγ2 gene expression in undifferentiated, BMP4 treated cells expressing control, full length Zfp423, or Zfp423 ΔSBD. (g) Expression of adipocyte selective mRNAs in cultures following BMP4-induced differentiation, and oil-red O staining of lipid accumulation in differentiated cultures. * denotes p<0.05 in Student’s T-test. n=3 replicates.