Figure 3.
Sdk protein colocalizes with F-actin and the WRC at vertices and LC–LC contacts. (A–F) Sdk::GFP localization relative to F-actin (A–A′), p-MyoII (B), SCAR (C–E), and mC::Abi (F). Sdk::GFP protein trap (green), SCAR (red), and E-cad (blue). (G) Cross-correlation analysis of pixels between Sdk::GFP and putative interacting proteins. Sdk::GFP shows the highest degree of colocalization with Actin, Abi, and SCAR at both 26 and 32 h APF. The lowest colocalizations are with SCAR at 40 h APF and with p-MyoII. The relative magnitudes of the Manders’ colocalization coefficients M1 and M2 show that Actin, Abi, and SCAR are more widely distributed relative to Sdk. n = 30 ommatidia in three eyes per experiment. Error bars represent SD. Scale bar, 10 μm.

Sdk protein colocalizes with F-actin and the WRC at vertices and LC–LC contacts. (A–F) Sdk::GFP localization relative to F-actin (A–A′), p-MyoII (B), SCAR (C–E), and mC::Abi (F). Sdk::GFP protein trap (green), SCAR (red), and E-cad (blue). (G) Cross-correlation analysis of pixels between Sdk::GFP and putative interacting proteins. Sdk::GFP shows the highest degree of colocalization with Actin, Abi, and SCAR at both 26 and 32 h APF. The lowest colocalizations are with SCAR at 40 h APF and with p-MyoII. The relative magnitudes of the Manders’ colocalization coefficients M1 and M2 show that Actin, Abi, and SCAR are more widely distributed relative to Sdk. n = 30 ommatidia in three eyes per experiment. Error bars represent SD. Scale bar, 10 μm.

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