Acetaldehyde dissociates the PTP1B-E-cadherin-β-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism

Parimal Sheth, Ankur Seth, Katherine J. Atkinson, Tarun Gheyi, Gautam Kale, Francesco Giorgianni, Dominic M. Desiderio, Chunying Li, Anjaparavanda Naren, Radhakrishna Rao

Research output: Contribution to journalArticle

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Abstract

Interactions between E-cadherin, β-catenin and PTP1B (protein tyrosine phosphatase 1B) are crucial for the organization of AJs (adherens junctions) and epithelial cell-cell adhesion. In the present study, the effect of acetaldehyde on the AJs and on the interactions between E-cadherin, β-catenin and PTP1B was determined in Caco-2 cell monolayers. Treatment of cell monolayers with acetaldehyde induced redistribution of E-cadherin and β-catenin from the intercellular junctions by a tyrosine phosphorylation-dependent mechanism. The PTPase activity associated with E-cadherin and β-catenin was significantly reduced and the interaction of PTP1B with E-cadherin and β-catenin was attenuated by acetaldehyde. Acetaldehyde treatment resulted in phosphorylation of β-catenin on tyrosine residues, and abolished the interaction of β-catenin with E-cadherin by a tyrosine kinase-dependent mechanism. Protein binding studies showed that the treatment of cells with acetaldehyde reduced the binding of β-catenin to the C-terminal region of E-cadherin. Pairwise binding studies using purified proteins indicated that the direct interaction between E-cadherin and β-catenin was reduced by tyrosine phosphorylation of β-catenin, but was unaffected by tyrosine phosphorylation of E-cadherin-C. Treatment of cells with acetaldehyde also reduced the binding of E-cadherin to GST (glutathione S-transferase)-PTP1B. The pairwise binding study showed that GST-E-cadherin-C binds to recombinant PTP1B, but this binding was significantly reduced by tyrosine phosphorylation of E-cadherin. Acetaldehyde increased the phosphorylation of β-catenin on Tyr-331, Tyr-333, Tyr-654 and Tyr-670. These results show that acetaldehyde induces disruption of interactions between E-cadherin, β-catenin and PTP1B by a phosphorylation-dependent mechanism.

Original languageEnglish (US)
Pages (from-to)291-300
Number of pages10
JournalBiochemical Journal
Volume402
Issue number2
DOIs
StatePublished - Mar 1 2007

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Non-Receptor Type 1 Protein Tyrosine Phosphatase
Catenins
Phosphorylation
Caco-2 Cells
Acetaldehyde
Cadherins
Monolayers
Tyrosine
Glutathione Transferase
Adherens Junctions
Cells
Protein Tyrosine Phosphatases
Intercellular Junctions
Cell adhesion
Recombinant Proteins
Protein Binding

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Acetaldehyde dissociates the PTP1B-E-cadherin-β-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism. / Sheth, Parimal; Seth, Ankur; Atkinson, Katherine J.; Gheyi, Tarun; Kale, Gautam; Giorgianni, Francesco; Desiderio, Dominic M.; Li, Chunying; Naren, Anjaparavanda; Rao, Radhakrishna.

In: Biochemical Journal, Vol. 402, No. 2, 01.03.2007, p. 291-300.

Research output: Contribution to journalArticle

Sheth, Parimal ; Seth, Ankur ; Atkinson, Katherine J. ; Gheyi, Tarun ; Kale, Gautam ; Giorgianni, Francesco ; Desiderio, Dominic M. ; Li, Chunying ; Naren, Anjaparavanda ; Rao, Radhakrishna. / Acetaldehyde dissociates the PTP1B-E-cadherin-β-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism. In: Biochemical Journal. 2007 ; Vol. 402, No. 2. pp. 291-300.
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AU - Gheyi, Tarun

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AU - Giorgianni, Francesco

AU - Desiderio, Dominic M.

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