Skip to main content
. 2015 Oct 2;6(34):36762–36773. doi: 10.18632/oncotarget.5461

Figure 4. CD44 signaling promotes the phosphorylation of cytoskeletal proteins cortactin and paxillin.

Figure 4

A. Panel of immunoblots comparing the expression and phosphorylation status of the kinases Src and FAK in the parental and bone-tropic MDA-MB-231 cell lines. B. Immunoblots comparing the expression and phosphorylation status of Src and FAK following stimulation of MDA-MB-231BO cells with HA. C. Panel of immunoblots comparing the expression and phosphorylation status of the cytoskeletal proteins cortactin and paxillin in MDA-MB-231 (left panel) and Hs578T (right panel) breast cancer cell lines. D. Immunoblot comparing the basal expression and phosphorylation status of cortactin and paxillin in parental MDA-MB-231 and bone-tropic MDA-MB-231BO cells. E. Panel of immunoblots illustrating the levels of phosphorylation detected in paxillin in response to HA stimulation of MDA-MB-231 cells in the absence or presence of CD44 (left panel) or the absence and presence of cortactin (CTTN). F. Immunoblots measuring the levels of cortactin phospgorylation in HA-stimulated MDA-MB-2331 cells in the absence or presence of a neutralizing antibody to β1-integrin receptors. Equal protein loading in all immunoblots is confirmed by reanalysis of GAPDH expression. Blots shown in A-F are representative of at least three independent experiments.