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Fig. 6. Myosin IIA is a Dg partner in notochord. (A) Immunoprecipitation (IPP) using an antibody against β-Dg. The precipitate and supernatant of wild-type (WT) and Dg-MO-injected notochords were subjected to western blotting with antibodies against myosin IIA and β-Dg. (B) Identification of Dg and myosin IIA localization using immunofluorescence confocal microscopy. Colocalization of Dg and myosin IIA is observed at cell cortices at stage 28 in WT embryos. (C) Immunodetection of myosin IIA (a,b) and Tor70 proteins (c,d) in C-MO and Dg-MO notochords. Labeling of myosin IIA was lost in Dg morphants at stage 32. Nuclei are stained with Hoechst (blue). (D) Protein extracts of WT, Dg-MO and myosin IIA-MO embryos were subjected to western blotting with antibodies against myosin IIA, actin and α-tubulin (6% SDS-PAGE) and with an antibody against β-Dg (12% SDS-PAGE). In Dg-MO extracts, Dg expression was strongly decreased, whereas the amount of myosin IIA was comparable to that of controls. Note that the decrease in Dg and myosin is not accompanied by a decrease in α-tubulin (α-Tub) or actin. R, ratios of myosin IIA, β-Dg and actin to α-tubulin normalized to WT. Scale bars: 25 µm in B,C.
Image published in: Buisson N et al. (2014)
Copyright © 2014. Image reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.
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