Unknown

Dataset Information

0

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

Json Xml
altmetric image

Publications

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]

Similar Datasets

Unknown bFGF-mediated phosphorylation of δ-catenin increases its protein stability and the ability to induce the nuclear redistribution of β-catenin.
| S-EPMC8414378 | biostudies-literature
Unknown Interaction of EGFR to δ-catenin leads to δ-catenin phosphorylation and enhances EGFR signaling.
| S-EPMC4756308 | biostudies-literature
Unknown Phosphorylation Reduces the Mechanical Stability of the ?-Catenin/ ?-Catenin Complex.
| S-EPMC6916283 | biostudies-literature
Unknown Phosphorylation of TOPK at Y74, Y272 by Src increases the stability of TOPK and promotes tumorigenesis of colon.
| S-EPMC5029716 | biostudies-literature
Unknown δ-Catenin Increases the Stability of EGFR by Decreasing c-Cbl Interaction and Enhances EGFR/Erk1/2 Signaling in Prostate Cancer.
| S-EPMC5935102 | biostudies-literature
Unknown Tyrosine phosphorylation of LRP6 by Src and Fer inhibits Wnt/β-catenin signalling.
| S-EPMC4264928 | biostudies-literature
Unknown Deuteration of the farnesyl terminal methyl groups of δ-tocotrienol and its effects on the metabolic stability and ability of inducing G-CSF production.
| S-EPMC7433030 | biostudies-literature
Unknown AKR1B10 promotes breast cancer metastasis through integrin α5/δ-catenin mediated FAK/Src/Rac1 signaling pathway.
| S-EPMC5190059 | biostudies-literature
Unknown Anti-angiogenic therapy increases intratumoral adenovirus distribution by inducing collagen degradation.
| S-EPMC3443547 | biostudies-literature
Unknown NFATc1 phosphorylation by DYRK1A increases its protein stability.
| S-EPMC5325557 | biostudies-other