Three-Dimensional Structure of the Armadillo Repeat Region of β-Catenin

@article{Huber1997ThreeDimensionalSO,
  title={Three-Dimensional Structure of the Armadillo Repeat Region of $\beta$-Catenin},
  author={Andrew H. Huber and William James Nelson and William I. Weis},
  journal={Cell},
  year={1997},
  volume={90},
  pages={871-882}
}

Figures and Tables from this paper

Crystal Structure of a Full-Length β -Catenin
TLDR
The crystal structures of full-length zebrafish β -catenin and a human β -Catenin fragment that contains both the armadillo repeat and the C-terminal domains reveal the existence of a long α helix that forms part of the β catenin superhelical core.
Crystal Structure of a β-Catenin/Tcf Complex
Crystal structure of a full-length beta-catenin.
Structure of a human Tcf4–β-catenin complex
TLDR
The crystal structure of a human Tcf4–β- catenin complex is described and it is compared with recent structures of β-catenin in complex with Xenopus Tcf3 (XTcf3) and mammalian E-cadherin to reveal anticipated similarities with the closely related XTcf3 complex but unexpectedly lacks one component observed in the XTcf2 structure.
The Terminal Region of β-Catenin Promotes Stability by Shielding the Armadillo Repeats from the Axin-scaffold Destruction Complex*
TLDR
It is shown that forms of β-catenin lacking the unstructured C-terminal domain (CTD) show faster turnover than full-length or minimally truncated β- catenins, and that Amino acids 733–759 are critical for β-Catenin FRET activity and stability.
Multivalent Interaction of Beta-Catenin With its Intrinsically Disordered Binding Partner Adenomatous Polyposis Coli
TLDR
A combination of single-site substitutions, deletions and insertions are used to dissect the mechanism of molecular recognition and the roles of the three β-catenin-binding subdomains of APC, both at equilibrium and under kinetic conditions.
Mechanistic insights from structural studies of β-catenin and its binding partners
TLDR
Structural and biochemical studies provide important insights into β-catenin-mediated mechanisms of cell adhesion and Wnt signaling and suggest potential approaches for the design of therapeutic agents to treat diseases caused by misregulated β- catenin expression.
Crystal structure of a -catenin/Axin complex suggests a mechanism for the -catenin destruction complex
TLDR
It is proposed that a key function of APC in the -catenin destruction complex is to remove phosphorylated -Catenin product from the active site.
Molecular mechanisms of β‐catenin recognition by adenomatous polyposis coli revealed by the structure of an APC–β‐catenin complex
TLDR
The crystal structure of a 15 amino acid β‐Catenin binding repeat from APC bound to the armadillo repeat region of β‐catenin is determined, which suggests that the 20 amino acid repeats can adopt two modes of binding to β‐ catenin.
Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex.
TLDR
It is proposed that a key function of APC in the beta-catenin destruction complex is to remove phosphorylated beta-Catenin product from the active site.
...
...

References

SHOWING 1-10 OF 97 REFERENCES
Functional interaction of β-catenin with the transcription factor LEF-1
TLDR
β-catenin regulates gene expression by direct interaction with transcription factors such as LEF-1, providing a molecular mechanism for the transmission of signals from cell-adhesion components or wnt protein to the nucleus.
Binding of GSK3β to the APC-β-Catenin Complex and Regulation of Complex Assembly
TLDR
It is shown that when β-catenin is present in excess, APC binds to another component of the WINGLESS pathway, glycogen synthase kinase 3β (GSK3β), a mammalian homolog of Drosophila ZESTE WHITE 3, which was a good substrate for GSK3β in vitro and the phosphorylation sites were mapped to the central region of APC.
Drosophila α-Catenin and E-cadherin Bind to Distinct Regions of Drosophila Armadillo*
TLDR
The data complement and extend results obtained in studies of vertebrate adherens junctions, providing a foundation for understanding how junctional proteins assemble and a basis for interpreting existing mutations and creating new ones.
E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton
TLDR
It is shown that the APC tumor suppressor gene product forms strikingly similar associations as found in cell junctions and suggested that beta-catenin and plakoglobin are central regulators of cell adhesion, cytoskeletal interaction, and tumor suppression.
Stabilization of β-Catenin by Genetic Defects in Melanoma Cell Lines
TLDR
Genetic defects that result in up-regulation of β-catenin may play a role in melanoma progression.
Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
TLDR
It is suggested that catenins represent an important link between EGF-induced signal transduction and cadherin function.
An in vivo structure-function study of armadillo, the beta-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for wingless signaling
TLDR
The first in vivo structure-function study of an adherens junction protein is performed, by generating and examining a series of Armadillo mutants in the context of the entire animal, and it is demonstrated that Armadillos roles in ad herens junctions and Wingless signaling are independent.
A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated.
TLDR
E-cadherin-catenin interaction may be regulated by phosphorylation of the catenin-binding domain, which might represent one molecular mechanism to regulate cadherin mediated cell adhesion.
...
...