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C-Src-mediated phosphorylation of ?-catenin increases its protein stability and the ability of inducing nuclear distribution of ?-catenin.

ABSTRACT: Although ?-catenin was first considered as a brain specific protein, strong evidence of ?-catenin overexpression in various cancers, including prostate cancer, has been accumulated. Phosphorylation of ?-catenin by Akt and GSK3? has been studied in various cell lines. However, tyrosine phosphorylation of ?-catenin in prostate cancer cells remains unknown. In the current study, we demonstrated that Src kinase itself phosphorylates ?-catenin on its tyrosine residues in prostate cancer cells and further illustrated that Y1073, Y1112 and Y1176 of ?-catenin are predominant sites responsible for tyrosine phosphorylation mediated by c-Src. Apart from c-Src, other Src family kinases, including Fgr, Fyn and Lyn, can also phosphorylate ?-catenin. We also found that c-Src-mediated Tyr-phosphorylation of ?-catenin increases its stability via decreasing its affinity to GSK3? and enhances its ability of inducing nuclear distribution of ?-catenin through interrupting the integrity of the E-cadherin. Taken together, these results indicate that c-Src can enhance the oncogenic function of ?-catenin in prostate cancer cells.

SUBMITTER: He Y 

PROVIDER: S-EPMC4074208 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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C-Src-mediated phosphorylation of δ-catenin increases its protein stability and the ability of inducing nuclear distribution of β-catenin.

He Yongfeng Y   Kim Hangun H   Ryu Taeyong T   Lee Kwang-Youl KY   Choi Won-Seok WS   Kim Kyeong-Man KM   Zheng Mei M   Joh Yechan Y   Lee Jae-Hyuk JH   Kwon Dong-Deuk DD   Lu Qun Q   Kim Kwonseop K  

Biochimica et biophysica acta 20140109 4

Although δ-catenin was first considered as a brain specific protein, strong evidence of δ-catenin overexpression in various cancers, including prostate cancer, has been accumulated. Phosphorylation of δ-catenin by Akt and GSK3β has been studied in various cell lines. However, tyrosine phosphorylation of δ-catenin in prostate cancer cells remains unknown. In the current study, we demonstrated that Src kinase itself phosphorylates δ-catenin on its tyrosine residues in prostate cancer cells and fur  ...[more]

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