Chromosomal translocation between 9 and 22 chromosomes leads to the fusion of bcr and abl genes. Because of different breakpoints in bcr gene three forms of chimeric BCR-ABL proteins exist – p230, p210, and p190. BCR-ABLp190 lacks Pleckstrin homology (PH) domain of BCR and is associated with acute lymphoblastic leukaemia. In contrast, BCR-ABLp210 has PH domain and occurs during chronic myeloblastic leukaemia. BCR-ABL can bind to centrosomes, which function as a regulating center of cell division and spindle formation during mitosis. Cortactin, the main function of which is actin branching, was previously identified by mass-spectrometry as one of the potential partners interacting with the PH domain of BCR. Aim. To determine whether BCR and cortactin colocalize with centrosomes and to study a possible role of PH domain in such colocalization. Methods. Mammalian cell culturing, immunofluorescence analysis, fluorescent microscopy of live cells. Results. In the present work we show that both full-length BCR protein and PH domain colocalize with centrosome together with cortactin in live HEK293T cells. We also demonstrate that BCR colocalizes with γ-tubulin and the points of actin branching in fixed K562 cells. Using anti-ABL and anti-BCR antibodies we also show that colocalization with the actin branching center is typical for BCR-ABL and BCR, but not for ABL alone. Conclusions. PH domain of BCR is required for colocalization of BCR or BCR-ABL with centrosome. Together with cortactin, BCR-ABL can affect centrosome function through deregulation of actin branching or abnormal phosphorylation, which can be a matter of further research.