Caveolin-1 interacts with protein phosphatase 5 and modulates its activity in prostate cancer cells
書誌事項
- 公開日
- 2013-02
- 資源種別
- journal article
- 権利情報
-
- https://www.elsevier.com/tdm/userlicense/1.0/
- https://www.elsevier.com/legal/tdmrep-license
- https://doi.org/10.15223/policy-017
- https://doi.org/10.15223/policy-037
- https://doi.org/10.15223/policy-012
- https://doi.org/10.15223/policy-029
- https://doi.org/10.15223/policy-004
- DOI
-
- 10.1016/j.bbrc.2013.01.051
- 公開者
- Elsevier BV
この論文をさがす
説明
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.
収録刊行物
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- Biochemical and Biophysical Research Communications
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Biochemical and Biophysical Research Communications 431 (4), 724-728, 2013-02
Elsevier BV
