Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochim Biophys Acta. 2014 Apr;1843(4):758-68. doi: 10.1016/j.bbamcr.2013.12.021. Epub 2014 Jan 9.

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

Author information

  • 1College of Pharmacy, Research Institute for Drug Development, Chonnam National University, Gwangju, South Korea.
  • 2College of Pharmacy, Research Institute of Life and Pharmaceutical Sciences, Sunchon National University, Sunchon, South Korea.
  • 3School of Biological Sciences and Technology, College of Natural Sciences, College of Medicine, Chonnam National University, Gwangju, South Korea.
  • 4Chonnam National University Hospital, Gwangju, South Korea.
  • 5Department of Anatomy and Cell Biology, The Brody School of Medicine, East Carolina University, Greenville, USA.
  • 6College of Pharmacy, Research Institute for Drug Development, Chonnam National University, Gwangju, South Korea; Chonnam National University Hospital, Gwangju, South Korea. Electronic address: koskim@chonnam.ac.kr.

Abstract

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 further illustrated that Y1073, Y1112 and Y1176 of δ-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 δ-catenin. We also found that c-Src-mediated Tyr-phosphorylation of δ-catenin increases its stability via decreasing its affinity to GSK3β and enhances its ability of inducing nuclear distribution of β-catenin through interrupting the integrity of the E-cadherin. Taken together, these results indicate that c-Src can enhance the oncogenic function of δ-catenin in prostate cancer cells.

KEYWORDS:

E-cadherin; GSK3; Tyrosine phosphorylation; c-Src; δ-Catenin

PMID:
24412473
PMCID:
PMC4074208
DOI:
10.1016/j.bbamcr.2013.12.021
[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center