Association of Plakoglobin with APC, a Tumor-Suppressor Gene Product, and Its Regulation by Tyrosine Phosphorylation

Shibata, Takeo; Gotoh, Masahiro; Ochiai, Atsushi; Hirohashi, Setsuo

doi:10.1006/bbrc.1994.2213

Cited by 75 publications

(41 citation statements)

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“…Thus, it is logical that this cell -cell zipper would disappear concomitant with increased cellular invasion (Shibata et al, 1994). This disappearance of E-cadherin and/or any of the major adhesion components affiliated with it is noted in most advanced carcinoma cells (Takeichi, 1977;Hazan and Norton, 1998;Takeda et al, 1999).…”

Section: Discussionmentioning

confidence: 98%

“…These molecules not only play structural roles but also alter cell responses and phenotypes. b-Catenin is also found to immunoprecipitate with the APC tumour suppressor protein (Su et al, 1993;Hulsken et al, 1994;Shibata et al, 1994), and has been recently identified as an oncogene (Kim et al, 2002;Minamoto et al, 2002;Kielhorn et al, 2003;Schneider et al, 2003). It is also central to cell signalling, as upon dissociation from E-cadherin, it transits to the nucleus to alter transcriptional profiles (Mason et al, 2002;van de Wetering et al, 2002).…”

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confidence: 99%

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Luteinising hormone-releasing hormone analogue reverses the cell adhesion profile of EGFR overexpressing DU-145 human prostate carcinoma subline

2005

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Cetrorelix, a luteinising hormone-releasing hormone (LHRH) analogue, has been shown to limit growth of the human androgenindependent prostate cell line DU-145, although other inhibitory actions may also be affected. Both growth and invasion of DU-145 cells are linked to autocrine epidermal growth factor receptor (EGFR) signalling. Invasiveness requires not only cells to migrate to conduits, but also reduced adhesiveness between tumour cells to enable separation from the tumour mass. Thus, we investigated whether Cetrorelix alters the DU-145 cell -cell adhesion and if this occurs via altered EGFR signalling. Pharmacologic levels of Cetrorelix limited the invasiveness of a highly invasive DU-145 subline overexpressing full-length EGFR (DU-145 WT). Extended exposure of the cells to Cetrorelix resulted in increased levels of the cell -cell adhesion complex molecules E-cadherin, a-and bcatenin, and p120. Puromycin blocked the increases in E-cadherin and b-catenin levels, suggesting that de novo protein synthesis is required. The Cetrorelix effect appears to occur via transmodulation of EGFR by a protein kinase C (PKC)-dependent mechanism, as there were no changes in DU-145 cells expressing EGFR engineered to negate the PKC transattenuation site (DU-145 A654); downregulation of EGFR signalling produced a similar upregulation in adhesion complex proteins, further suggesting a role for autocrine signalling. Cetrorelix increased the cell -cell adhesiveness of DU-145 WT cells to an extent similar to that seen when autocrine EGFR signalling is blocked; as expected, DU-145 A654 cell -cell adhesion also was unaffected by Cetrorelix. The increased adhesiveness is expected as the adhesion complex molecules moved to the cells' periphery. These data offer direct insight into the possible crosstalk pathways between the LHRH and EGFR receptor signalling. The ability of Cetrorelix to downregulate EGFR signalling and subsequently reverse the antiadhesiveness found in metastatic prostate cancer highlights a novel potential target for therapeutic strategies.

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Section: Discussionmentioning

confidence: 98%

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confidence: 99%

Luteinising hormone-releasing hormone analogue reverses the cell adhesion profile of EGFR overexpressing DU-145 human prostate carcinoma subline

2005

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“…These membranes were incubated with radiolabeled fusion proteins in HBB buffer (20 mM Hepes, pH 7.5, 5.5 mM MgCl 2 , 1 mM KCl, 5 mM dithiothreitol, 10 mM glutathione) and washed with TPBS (0.2% Triton X-100 in phosphate-buffered saline) as described previously (21). After three rounds of screening, positive phages were isolated and digested with EcoRI, and the inserts were subcloned into pBSKII-SK (Stratagene) vector for sequence analysis.…”

Section: Methodsmentioning

confidence: 99%

Identification of Human Cadherin-14, a Novel Neurally Specific Type II Cadherin, by Protein Interaction Cloning

Shibata¹,

Shimoyama²,

Gotoh³

et al. 1997

Journal of Biological Chemistry

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Cadherins, a family of Ca 2؉ -dependent cell-cell adhesion molecules, mediate neural cell-cell interactions and may play important roles in neural development. By searching for molecules that interact with ␤-catenin, a cytoplasmic regulator of cadherins, we have identified a new member of the cadherin family, which we named human cadherin-14. Cadherin-14 had high amino acid sequence homology with the type II subgroup of cadherins and was broadly expressed in the central nervous system. Cadherin-14 is a novel neurally specific cell-cell adhesion molecule and may regulate neural morphogenesis.

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“…All the PCR products were sequenced. Glutathione-S-transferase (GST) fusion proteins were expressed in JM109, as described by Shibata et al (15).…”

Section: Generation Of Recombinant Proteins and In Vitro Bindingmentioning

confidence: 99%

Tyrosine-phosphorylation of the 12th armadillo-repeat of β-catenin is associated with cadherin dysfunction in human cancer

Ochiai¹

2009

Int J Oncol

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Abstract. Tyrosine phosphorylation of ß-catenin, an intracytoplasmic cadherin-binding protein, causes disruption of the cadherin-mediated cell adhesion system in cancer cells. We identified that the c-erbB-2 protein activated by TGF· was capable of binding to the 12th armadillo repeat (arm12) of ß-catenin with increased phosphorylation-state level. We produced a monoclonal antibody, 4G7, which recognizes a phosphorylated-tyrosine residue (Tyr-654) located at arm12 of ß-catenin. Tyrosine phosphorylation of the arm12 was detected after stimulation with TGF· in TMK-1. Immunoprecipitation analyses using 4G7, anti-ß-catenin, ·-catenin, the c-erbB-2 gene product and phosphotyrosine antibodies indicated that tyrosine phosphorylation of the arm12 was closely correlated with dissociation between E-cadherin/ ß-catenin and ·-catenin or the c-erbB-2 gene product, but not with dissociation between ß-catenin and E-cadherin. Immunocytochemical staining of TMK-1 cells using the 4G7 antibody revealed that tyrosine phosphorylation of the arm12 was localized at cell-cell contact sites of cancer cells transiently and only after TGF· treatment. Immunohistochemical localization of the 4G7 antibody was observed in cancer cells at the invasive front where they detached from cancer nests. These findings indicated that the tyrosine phosphorylation of arm12 is a key marker of cadherin dysfunction and the 4G7 antibody may be useful in screening for a ß-catenin phosphorylation ligand or tyrosine kinases.

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Association of Plakoglobin with APC, a Tumor-Suppressor Gene Product, and Its Regulation by Tyrosine Phosphorylation

Cited by 75 publications

References 0 publications

Luteinising hormone-releasing hormone analogue reverses the cell adhesion profile of EGFR overexpressing DU-145 human prostate carcinoma subline

Luteinising hormone-releasing hormone analogue reverses the cell adhesion profile of EGFR overexpressing DU-145 human prostate carcinoma subline

Identification of Human Cadherin-14, a Novel Neurally Specific Type II Cadherin, by Protein Interaction Cloning

Tyrosine-phosphorylation of the 12th armadillo-repeat of β-catenin is associated with cadherin dysfunction in human cancer

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