PRL-3 interacts with integrin β1 and decreases its tyrosine phosphorylation in LoVo cells. (A) PRL-3 interacted with integrin β1. Equal amount of lysates (500 μg of protein) from LoVo-P cells, which stably expressed myc-tagged human PRL-3, and control LoVo-C cells were immunoprecipitated with anti-myc antibody, followed by Western blot with anti-integrin β1 antibody and anti-PRL-3 antibody. Expression of integrin β1 and PRL-3 in the lysates (50 μg of protein) was shown as Input. GAPDH protein expression was shown as a loading control. Molecular weight was shown. (B) PRL-3 was colocalized with integrin β1. LoVo cells were transiently transfected with GFP-PRL-3 (green). Twenty-four hours after transfection, cells were fixed, stained with an anti-integrin β1 antibody (red), and observed under a laser confocal microscope. The white arrow in Merge (4×) indicates the colocalization of PRL-3 with integrin β1 (yellow). (C) PRL-3 decreased tyrosine phosphorylated integrin β1. Equal amount of lysates (500 μg of preotein) from LoVo-C and LoVo-P cells were immunoprecipitated with anti-phosphotyrosine antibody or IgG control. The precipitates were subjected to Western blot with anti-integrin β1.