Caveolin-1 interacts with protein phosphatase 5 and modulates its activity in prostate cancer cells.
Caveolin-1 is highly expressed in prostate cancer cells, and is implicated in disease progression. Here, we identified protein phosphatase 5 (PP5) as a novel cellular binding partner of caveolin-1 using a pull-down approach in combination with mass spectrometry-based proteomic analyses. In situ proximity ligation assays demonstrated co-localization and physical interaction of caveolin-1 and PP5 in the cytoplasm of PC-3 human prostate cancer cells. Using yeast two-hybrid analysis, we found that caveolin-1 interacted with the catalytic domain of PP5. We also found that PP5 activity was elevated about 1.7-fold in the presence of 2 μM caveolin-1, and that the scaffolding domain of caveolin-1 is required for this activation. Our results suggest that caveolin-1 is a novel physiological activator of PP5.
Department of Chemistry, Kurume University School of Medicine, Kurume 830-0011, Japan.
Junichi
J
Taira
Yuichiro
Y
Higashimoto
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D051242:Caveolin 1 / Q000378:metabolism*; D045744:Cell Line, Tumor; D004789:Enzyme Activation; D006801:Humans; D008297:Male; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism*; D011471:Prostatic Neoplasms / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D051242:Caveolin 1; D009687:Nuclear Proteins; D010749:Phosphoprotein Phosphatases; C089641:protein phosphatase 5