Fig. 2: Liprin-α1 directs cytoplasmic B56γ at PMAPs.

MDA-MB-231 cells expressing B56γ-GFP treated with saponin and fixed with PFA and immunostained. a–d Accumulation of B56γ-GFP in ERC1-positive PMAPs, in the presence of control siRNA (siCtr) or anti-liprin-α1 siRNA (siLip). a Representative confocal images. b Quantification of the liprin-α1-derived fluorescence in ERC1-positive PMAPs, expressed as Liprin-α1/ERC1 ratio, revealed efficient silencing of Liprin-α1 in cells cotransfected with B56γ-GFP and siLip. c Quantification of B56γ-GFP in ERC1-positive PMAPs, represented as a ratio of the intensity of the two proteins, as revealed by immunofluorescence. d Quantification of B56γ-GFP signal in PMAPs in respect to its expression level, as determined by the fluorescence in the nucleus. e–h Accumulation of B56γ-GFP in Liprin-α1-positive PMAPs, in the presence of control siRNA (siCtr) or anti-ERC1 siRNA (siERC1). e Representative confocal images. f Quantification of B56γ-GFP in liprin-α1-positive PMAPs, represented as a ratio of the intensity of the two proteins, as revealed by immunofluorescence. g Quantification of the B56γ-GFP signal in PMAPs in respect to its expression level, as determined by the fluorescence in the nucleus. h Quantification of the ERC1-derived fluorescence in liprin-α1-positive PMAPs, expressed as ERC1/liprin-α1 ratio, revealed efficient silencing of ERC1 in cells cotransfected with B56γ-GFP and siERC1. eLip, endogenous liprin; eERC1, endogenous ERC1; the same contrast was applied to confocal images in (a and e).