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Fig. 1 | Journal of Experimental & Clinical Cancer Research

Fig. 1

From: Cleavage of tropomodulin-3 by asparagine endopeptidase promotes cancer malignancy by actin remodeling and SND1/RhoA signaling

Fig. 1

AEP binds to Tmod3 and specifically cleaves Tmod3 at N157. A Left panel: silver-stained gel showing immunoprecipitated AEP or lgG and their bound proteins from mouse embryonic fibroblasts (MEFs); right panel: immunoblot showing Tmod3 exists in AEP immunoprecipitants. Arrowhead indicates Tmod3. B Mass spectrometry analysis of proteins interacting with AEP. The detected MS/MS peptide spectra of Tmod3 are shown. C Endogenous co-IP and western blotting of the AEP/Tmod3 interaction in U87-MG and A172 cells. D Representative confocal images showing the colocalization of AEP (red) and Tmod3 (green) in U87-MG and A172 cells by immunofluorescent staining. Scale bar, 20 μm. Co-localization tracer profile along the line (white arrows) is indicated as merged image (right panel). E Immunoblots of Tmod3, AEP and GAPDH in A172, U87-MG and U251-MG cells with or without AEP OE. NC = negative control, cells expressing empty vector, OE = overexpression. F Immunoblots of Flag-tagged Tmod3, AEP and GAPDH in HEK293 cells co-transfected with Flag-Tmod3 and wild-type AEP or the AEP C189S mutant. NC, negative control, cells transfected with empty vector. G Immunoblots of Flag-tagged Tmod3, AEP and GAPDH in HEK293 cells co-transfected with AEP and panels of Tmod3 point mutants. H Tmod3 amino acid sequence alignment among different species. I Emulated domains of Tmod3-GSSN- interacting with AEP enzymatic center. Green (AEP enzymatic center), yellow sticks (Tmod3-GSSN-)

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