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Armc8 is a evolutionarily conserved armadillo protein involved in cell-cell adhesion complexes through multiple molecular interactions

Ismail Sahin Gül (UGent) , Paco Hulpiau (UGent) , Ellen Sanders (UGent) , Frans Van Roy (UGent) and Jolanda van Hengel (UGent)
(2019) BIOSCIENCE REPORTS. 39(8).
Author
Organization
Abstract
Armadillo-repeat-containing protein 8 (Armc8) belongs to the family of armadillo-repeat containing proteins, which have been found to be involved in diverse cellular functions including cell-cell contacts and intracellular signaling. By comparative analyses of armadillo repeat protein structures and genomes from various premetazoan and metazoan species, we identified orthologs of human Armc8 and analyzed in detail the evolutionary relationship of Armc8 genes and their encoded proteins. Armc8 is a highly ancestral armadillo protein although not present in yeast. Consequently, Armc8 is not the human ortholog of yeast Gid5/Vid28. Further, we performed a candidate approach to characterize new protein interactors of Armc8. Interactions between Armc8 and specific delta-catenins (plakophilins-1, -2, -3 and p0071) were observed by the yeast two-hybrid approach and confirmed by co-immunoprecipitation and co-localization. We also showed that Armc8 interacts specifically with alpha E-catenin but neither with alpha N-catenin nor with alpha T-catenin. Degradation of alpha E-catenin has been reported to be important in cancer and to be regulated by Armc8. A similar process may occur with respect to plakophilins in desmosomes. Deregulation of desmosomal proteins has been considered to contribute to tumorigenesis.
Keywords
ALPHA-T-CATENIN, AREA COMPOSITA, DEGRADATION, DESMOSOMES, BINDING, PROGRESSION, CARCINOMA, PROMOTES, FAMILY, FRUCTOSE-1, 6-BISPHOSPHATASE

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Citation

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MLA
Gül, Ismail Sahin, et al. “Armc8 Is a Evolutionarily Conserved Armadillo Protein Involved in Cell-Cell Adhesion Complexes through Multiple Molecular Interactions.” BIOSCIENCE REPORTS, vol. 39, no. 8, 2019, doi:10.1042/bsr20180604.
APA
Gül, I. S., Hulpiau, P., Sanders, E., Van Roy, F., & van Hengel, J. (2019). Armc8 is a evolutionarily conserved armadillo protein involved in cell-cell adhesion complexes through multiple molecular interactions. BIOSCIENCE REPORTS, 39(8). https://doi.org/10.1042/bsr20180604
Chicago author-date
Gül, Ismail Sahin, Paco Hulpiau, Ellen Sanders, Frans Van Roy, and Jolanda van Hengel. 2019. “Armc8 Is a Evolutionarily Conserved Armadillo Protein Involved in Cell-Cell Adhesion Complexes through Multiple Molecular Interactions.” BIOSCIENCE REPORTS 39 (8). https://doi.org/10.1042/bsr20180604.
Chicago author-date (all authors)
Gül, Ismail Sahin, Paco Hulpiau, Ellen Sanders, Frans Van Roy, and Jolanda van Hengel. 2019. “Armc8 Is a Evolutionarily Conserved Armadillo Protein Involved in Cell-Cell Adhesion Complexes through Multiple Molecular Interactions.” BIOSCIENCE REPORTS 39 (8). doi:10.1042/bsr20180604.
Vancouver
1.
Gül IS, Hulpiau P, Sanders E, Van Roy F, van Hengel J. Armc8 is a evolutionarily conserved armadillo protein involved in cell-cell adhesion complexes through multiple molecular interactions. BIOSCIENCE REPORTS. 2019;39(8).
IEEE
[1]
I. S. Gül, P. Hulpiau, E. Sanders, F. Van Roy, and J. van Hengel, “Armc8 is a evolutionarily conserved armadillo protein involved in cell-cell adhesion complexes through multiple molecular interactions,” BIOSCIENCE REPORTS, vol. 39, no. 8, 2019.
@article{8588400,
  abstract     = {{Armadillo-repeat-containing protein 8 (Armc8) belongs to the family of armadillo-repeat containing proteins, which have been found to be involved in diverse cellular functions including cell-cell contacts and intracellular signaling. By comparative analyses of armadillo repeat protein structures and genomes from various premetazoan and metazoan species, we identified orthologs of human Armc8 and analyzed in detail the evolutionary relationship of Armc8 genes and their encoded proteins. Armc8 is a highly ancestral armadillo protein although not present in yeast. Consequently, Armc8 is not the human ortholog of yeast Gid5/Vid28. Further, we performed a candidate approach to characterize new protein interactors of Armc8. Interactions between Armc8 and specific delta-catenins (plakophilins-1, -2, -3 and p0071) were observed by the yeast two-hybrid approach and confirmed by co-immunoprecipitation and co-localization. We also showed that Armc8 interacts specifically with alpha E-catenin but neither with alpha N-catenin nor with alpha T-catenin. Degradation of alpha E-catenin has been reported to be important in cancer and to be regulated by Armc8. A similar process may occur with respect to plakophilins in desmosomes. Deregulation of desmosomal proteins has been considered to contribute to tumorigenesis.}},
  articleno    = {{BSR20180604}},
  author       = {{Gül, Ismail Sahin and Hulpiau, Paco and Sanders, Ellen and Van Roy, Frans and van Hengel, Jolanda}},
  issn         = {{0144-8463}},
  journal      = {{BIOSCIENCE REPORTS}},
  keywords     = {{ALPHA-T-CATENIN,AREA COMPOSITA,DEGRADATION,DESMOSOMES,BINDING,PROGRESSION,CARCINOMA,PROMOTES,FAMILY,FRUCTOSE-1,6-BISPHOSPHATASE}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{12}},
  title        = {{Armc8 is a evolutionarily conserved armadillo protein involved in cell-cell adhesion complexes through multiple molecular interactions}},
  url          = {{http://dx.doi.org/10.1042/bsr20180604}},
  volume       = {{39}},
  year         = {{2019}},
}
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