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Figure 6. BOC variants show defective cell surface localization and impaired binding with <t>SHH</t> and PTCH1. (A) p.R407W and p.R681X variants dislocate BOC from the cell surface to the cytoplasm. Hela cells transfected with HA-tagged WT or mutant BOC were processed for immunofluorescence analysis with an HA antibody. p.R407W and p.R681X BOC are diffused in the cytoplasm, while the WT BOC, as well as p.G436S and p.D1018N BOC, is localized on the membrane. Nuclear nucleus was stained with Hoechst. Scale bar, 20um. (B) p.R681X variant results in a secreted protein. HEK293T cells were transfected with WT or mutant BOC. 24 h later, cells were serum starved for 20 h. Cell lysate and concentrated medium were analyzed by Western blotting with an HA antibody. 𝛽-actin served as a loading control. (C) Effective secretion of <t>SHH</t> <t>protein.</t> The experiment was performed as in B, except that a Flag-tagged SHH construct was used. (D) p.R407W and p.R681X variants weaken the binding of BOC to SHH. Conditioned media of SHH-Flag was incubated with conditioned media of extracellular domains (ECD) of WT or mutant BOC, followed by a pull-down assay with a Flag antibody. The WT or mutant BOC-ECD protein bound on the beads was analyzed by Western blotting with an HA antibody. Note that the p.D1018N variant was not analyzed because of the localization of D1018 in the cytoplasmic tail, but not ECD. (E) p.R407W, p.G436S and p.D1018N variants dampen the binding to BOC to
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Figure 6. BOC variants show defective cell surface localization and impaired binding with <t>SHH</t> and PTCH1. (A) p.R407W and p.R681X variants dislocate BOC from the cell surface to the cytoplasm. Hela cells transfected with HA-tagged WT or mutant BOC were processed for immunofluorescence analysis with an HA antibody. p.R407W and p.R681X BOC are diffused in the cytoplasm, while the WT BOC, as well as p.G436S and p.D1018N BOC, is localized on the membrane. Nuclear nucleus was stained with Hoechst. Scale bar, 20um. (B) p.R681X variant results in a secreted protein. HEK293T cells were transfected with WT or mutant BOC. 24 h later, cells were serum starved for 20 h. Cell lysate and concentrated medium were analyzed by Western blotting with an HA antibody. 𝛽-actin served as a loading control. (C) Effective secretion of <t>SHH</t> <t>protein.</t> The experiment was performed as in B, except that a Flag-tagged SHH construct was used. (D) p.R407W and p.R681X variants weaken the binding of BOC to SHH. Conditioned media of SHH-Flag was incubated with conditioned media of extracellular domains (ECD) of WT or mutant BOC, followed by a pull-down assay with a Flag antibody. The WT or mutant BOC-ECD protein bound on the beads was analyzed by Western blotting with an HA antibody. Note that the p.D1018N variant was not analyzed because of the localization of D1018 in the cytoplasmic tail, but not ECD. (E) p.R407W, p.G436S and p.D1018N variants dampen the binding to BOC to
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Figure 6. BOC variants show defective cell surface localization and impaired binding with SHH and PTCH1. (A) p.R407W and p.R681X variants dislocate BOC from the cell surface to the cytoplasm. Hela cells transfected with HA-tagged WT or mutant BOC were processed for immunofluorescence analysis with an HA antibody. p.R407W and p.R681X BOC are diffused in the cytoplasm, while the WT BOC, as well as p.G436S and p.D1018N BOC, is localized on the membrane. Nuclear nucleus was stained with Hoechst. Scale bar, 20um. (B) p.R681X variant results in a secreted protein. HEK293T cells were transfected with WT or mutant BOC. 24 h later, cells were serum starved for 20 h. Cell lysate and concentrated medium were analyzed by Western blotting with an HA antibody. 𝛽-actin served as a loading control. (C) Effective secretion of SHH protein. The experiment was performed as in B, except that a Flag-tagged SHH construct was used. (D) p.R407W and p.R681X variants weaken the binding of BOC to SHH. Conditioned media of SHH-Flag was incubated with conditioned media of extracellular domains (ECD) of WT or mutant BOC, followed by a pull-down assay with a Flag antibody. The WT or mutant BOC-ECD protein bound on the beads was analyzed by Western blotting with an HA antibody. Note that the p.D1018N variant was not analyzed because of the localization of D1018 in the cytoplasmic tail, but not ECD. (E) p.R407W, p.G436S and p.D1018N variants dampen the binding to BOC to

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Exome Sequencing Reveals the Genetic Architecture of Non-syndromic Orofacial Clefts and Identifies BOC as a Novel Causal Gene.

doi: 10.1002/advs.202412073

Figure Lengend Snippet: Figure 6. BOC variants show defective cell surface localization and impaired binding with SHH and PTCH1. (A) p.R407W and p.R681X variants dislocate BOC from the cell surface to the cytoplasm. Hela cells transfected with HA-tagged WT or mutant BOC were processed for immunofluorescence analysis with an HA antibody. p.R407W and p.R681X BOC are diffused in the cytoplasm, while the WT BOC, as well as p.G436S and p.D1018N BOC, is localized on the membrane. Nuclear nucleus was stained with Hoechst. Scale bar, 20um. (B) p.R681X variant results in a secreted protein. HEK293T cells were transfected with WT or mutant BOC. 24 h later, cells were serum starved for 20 h. Cell lysate and concentrated medium were analyzed by Western blotting with an HA antibody. 𝛽-actin served as a loading control. (C) Effective secretion of SHH protein. The experiment was performed as in B, except that a Flag-tagged SHH construct was used. (D) p.R407W and p.R681X variants weaken the binding of BOC to SHH. Conditioned media of SHH-Flag was incubated with conditioned media of extracellular domains (ECD) of WT or mutant BOC, followed by a pull-down assay with a Flag antibody. The WT or mutant BOC-ECD protein bound on the beads was analyzed by Western blotting with an HA antibody. Note that the p.D1018N variant was not analyzed because of the localization of D1018 in the cytoplasmic tail, but not ECD. (E) p.R407W, p.G436S and p.D1018N variants dampen the binding to BOC to

Article Snippet: 24 h after transfection, cells were serum starved for 12 h and then stimulated with 100 ng mL−1 SHH protein (R&D systems, #1845-SH) for 16 h. Cells were lysed in Passive Lysis Buffer (Promega) and Luciferase assays were performed with the Dual-Luciferase Reporter Assay System (Promega, #E1980) according to manufacturer’s instructions, using a Glomax Luminometer (Promega).

Techniques: Binding Assay, Transfection, Mutagenesis, Membrane, Staining, Variant Assay, Western Blot, Control, Construct, Incubation, Pull Down Assay