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. Author manuscript; available in PMC: 2013 Aug 3.
Published in final edited form as: Cell. 2012 Aug 3;150(3):620–632. doi: 10.1016/j.cell.2012.06.027

Figure 1. SirT1 deacetylates Pparγ in a ligand-dependent manner.

Figure 1

(A) Co-immunoprecipitation (Co-IP) of Flag-tagged SirT1 or HA-tagged Pparγ in response to overnight rosiglitazone treatment in 293 cells.

(B) Co-IP of Flag-Pparγ and SirT1 in 293 cells treated with troglitazone (Trog) or GW9662 (GW) overnight.

(C) Pparγ acetylation in 293 cells in response to resveratrol.

(D-E) In vitro Pparγ deacetylation by SirT1. Bovine serum albumin (BSA) is contained in the reaction buffer.

(F) Co-IP of Pparγ with SirT1 in mouse adipose tissues. We immunoprecipitated 2 mg of epididymal (eWAT) or inguinal fat lysates (iWAT) with Pparγ antibody H100, and blotted the immunoprecipitates with SirT1 or Pparγ (E8) antibodies.

(G) Co-IP of SirT1 and Pparγ with Flag M2 beads using iWAT (5 mg) from SirBACO mice expressing Flag-tagged SirT1.

See also Figure S1.