Extended Data Fig. 8: APPBP2 loss promotes PRDM16 protein stability and beige adipocyte biogenesis.
From: Post-translational control of beige fat biogenesis by PRDM16 stabilization
a, Changes in endogenous PRDM16 protein stability in control and Appbp2 KO inguinal adipocytes. PRDM16 protein levels were quantified by Image J software and normalized to β-actin levels. b, ChIP-qPCR analysis of PPARγ recruitment onto the PRDM16’s target loci in control and Appbp2 KO inguinal adipocytes. Ins1 was used as a nonspecific binding site. n = 3 per group. c, Left: Immunoblotting of indicated proteins in control and Appbp2 KO inguinal adipocytes. Right: Protein quantification normalized to β-actin levels. n = 3 per group. d, Relative mRNA levels of indicated genes in control and Appbp2 KO inguinal adipocytes in the presence or absence of forskolin. n = 3 per group. e, Mitochondrial DNA transcripts normalized to β-globin. n = 4 per group. f, OCR in control and Appbp2 KO adipocytes. OCR values were normalized by total protein (μg). n = 10 (Appbp2 KO), n = 9 (Control). Representative results in a and c from two independent experiments. Gel source data are presented in Supplementary Fig. 1. b–f, biologically independent samples. Data are mean ± s.e.m.; two-sided P values by unpaired Student’s t-test (b–e) or two-way repeated-measures ANOVA (f). * P < 0.05, *** P < 0.001. n.s., not significant. Exact P-values are in Supplementary Table 2.
