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. Author manuscript; available in PMC: 2015 Mar 17.
Published in final edited form as: Diabetes. 2014 Aug 11;64(1):299–310. doi: 10.2337/db14-0104

Figure 5. The perilipin-1 439fs mutant interacts with ABHD5 on the surface of lipid droplets.

Figure 5

Interaction between perilipin-1 (wild type (WT), 439fs or 398fs) and ABHD5 was assessed using bimolecular complementation (BiFC) in COS-7 cells after normalizing for equal expression of each protein. A) Yn-ABHD5 and Myc-PLIN1-Yc (wild type (WT), 439fs or 398fs mutants) were co-transfected in COS-7 cells and stained with anti-Myc and anti-mouse-Alexa594 for perilipin-1 (green) and DAPI for nuclei (blue). The presence of YFP BiFC signal indicates direct interaction between perilipin-1 and ABHD5; scale bar 10μm. B) The YFP BiFC signal was quantified as described in materials and methods. Results from three independent experiments are expressed as mean±SEM, where post hoc comparison is shown vs WT. ns-not significant ** P<0.001. C) The amount of Myc-perilipin-1 and ABHD5 expressed was assessed by immunoblotting. β-actin was used as a loading control.

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