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L~=Vwh?{Q6UΏ Ci;/ٙ~OGgfW}?7?KyiNX :x@xqq?8BIM!UAdobe PhotoshopAdobe Photoshop CS28BIMmaniIRFR8BIMAnDsnullAFStlongFrInVlLsObjcnullFrIDlong_^FStsVlLsObjcnullFsIDlongAFrmlongFsFrVlLslong_^LCntlong8BIMRoll8BIMmfrihttp://ns.adobe.com/xap/1.0/ 2013-05-31 GFP-tagged proteins containing the C-terminal third of human PNPLA5 localize to LDs.(A) Schematic of the domain structure of full length PNPLA5 highlighting the N-terminal catalytic dyad within the Patatin domain, the C-terminal basic patch region, and all truncation mutants generated. HeLa cells were treated overnight with OA, transfected with the indicated constructs for 24 h, fixed and stained with LipidTox Red, and then analyzed by fluorescence microscopy. N-terminal GFP-tagged PNPLA5 constructs missing the C-terminal third of the protein were found in the cytoplasm or nucleus (B, C, and E), whereas constructs containing the C-terminal third of PNPLA5 (residues 286–429), or one lacking a portion of the patatin domain localized to LipidTox stained LDs (D, F, and G). 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