Caveolin-1 interacts with protein phosphatase 5 and modulates its activity in prostate cancer cells

详细信息    查看全文

• 作者：Junichi Taira ; Yuichiro Higashimoto ; ^{higashiy@med.kurume-u.ac.jp}
• 关键词：Caveolin-1 ; Protein phosphatase 5 ; Prostate cancer ; Peptide mass fingerprinting
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2013
• 出版时间：22 February, 2013
• 年：2013
• 卷：431
• 期：4
• 页码：724-728
• 全文大小：459 K

文摘

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 ¦ÌM 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.