• Corpus ID: 42117849

Single amino acid substitutions in proteins of the armadillo gene family abolish their binding to alpha-catenin.

  title={Single amino acid substitutions in proteins of the armadillo gene family abolish their binding to alpha-catenin.},
  author={Hermann Aberle and Hillel Schwartz and Heinz Hoschuetzky and Rolf Kemler},
  journal={The Journal of biological chemistry},
  volume={271 3},
Analysis of the calcium-dependent cell adhesion molecule E-cadherin has led to the identification of catenins, which are necessary for cadherin function. Growing evidence that cadherins and catenins are subjected to genetic alterations in carcinogenesis makes it especially important to understand protein-protein interactions within the cadherin-catenin complex. Here we report the identification and analysis of the alpha-catenin binding site in plakoglobin (gamma-catenin). Using N- and C… 
Armc8 is an evolutionarily conserved armadillo protein involved in cell–cell adhesion complexes through multiple molecular interactions
Comparative analyses of armadillo repeat protein structures and genomes from various premetazoan and metazoan species identified orthologs of human Armc8 and analyzed in detail the evolutionary relationship of Arm c8 genes and their encoded proteins.
Protein kinase CKII regulates the interaction of β-catenin withα -catenin and its protein stability
It is concluded that CKII regulates the function of β-catenin in the cadherin adhesion complex as well as its cytoplasmic stability, which correlates with an enhanced cytosolic localization and a reduced association with the cytoskeleton of the mutant protein.
Protein kinase D1-mediated phosphorylation and subcellular localization of beta-catenin.
Evidence is provided that PKD1 interacts with and phosphorylates beta-Catenin at Thr(112) and Thr(120) residues in vitro and in vivo and provides a novel strategy to target beta-catenin function in cells including prostate cancer.
Parallel duplication and partial subfunctionalization of β-catenin/armadillo during insect evolution.
Providing first evidence of genetic separability of the cell adhesion and centrosome separation functions, the duplicated Tribolium and Acyrthosiphon arm paralogs offer new inroads for context-specific analyses of β-Catenin.
Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells.
Shrew-1 is introduced as a novel component of adherens junctions, interacting with E-cadherin-beta-catenin complexes in polarized epithelial cells.
Characterization of the Cadherin–Catenin Complex of the Sea Anemone Nematostella vectensis and Implications for the Evolution of Metazoan Cell–Cell Adhesion
The core function of the CCC as a link between cell adhesions and the actin cytoskeleton is ancestral in the eumetazoans, indicating that the basic organization of the complex is conserved across all metazoans.
Beta-Catenin Phosphorylated at Threonine 120 Antagonizes Generation of Active Beta-Catenin by Spatial Localization in trans-Golgi Network
In vitro and in vivo data unveil a previously unrecognized post-translational modification of ABC through T120 phosphorylation by PKD1, which alters subcellular localization and transcriptional activity of β-catenin.
Structure and biochemistry of cadherins and catenins.
It appears that alpha-catenin actively regulates the actin cytoskeleton at cadherin-based cell-cell contacts.
The cadherin–catenin complex as a focal point of cell adhesion and signalling: new insights from three‐dimensional structures
Structural studies on classic cadherins and these catenin molecules have provided new insight into the essential mechanisms underlying cadherin‐mediated cell interaction and caten in‐mediated cellular signalling.
BCL9-2 binds Arm/β-catenin in a Tyr142-independent manner and requires Pygopus for its function in Wg/Wnt signaling
The results suggest that the two proteins characterized, BCL9-2 and B9L, represent evolutionary duplicates of Legless, which have acquired distinct expression patterns while acting in a largely redundant manner.