Fig. 6
From: Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase
Localization and signaling network of Bcr-Abl p210, p190, FABD and PH mutant proteins. a Cellular localization of Bcr-Abl p210 and p190, p210 with the PH mutations R723A/K724A or R726A, with the FABD mutant F1100E, as well as a combination of PH and FABD mutation. Cells were fixed and immunostained with an anti-HA antibody (HA-Bcr-Abl). F-actin (actin) and nuclei (DNA) were stained with rhodamine-conjugated phalloidin and Hoechst, respectively. The white scale bar in the upper left image corresponds to 10 µm. b Quantification of co-localization of Bcr-Abl with actin fibers using ImageJ. The box-and-whisker plots show the median, lower/upper quartile, and minimum/maximum of % Actin co-localization for at least six quantified cells per Bcr-Abl mutant. c Representative immunoblot analysis of anti-Bcr-Abl/Abl immunoprecipitates from BaF3 cells stably transduced with the indicated Bcr-Abl variants. Fractions of the immunoprecipitates were immunoblotted for Bcr-Abl and its interaction partner Sts1. d Quantification of the co-immunoprecipitation of Sts1 with Bcr-Abl. The quantified amount of co-immunoprecipitated Sts1 after correction for the Bcr-Abl amounts is shown. Means ± s.d. of two biological replicates analyzed in two technical replicates
