The Structure of the β-Catenin/E-Cadherin Complex and the Molecular Basis of Diverse Ligand Recognition by β-Catenin

By A. H. Huber, William I. Weis. 2001

689 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c6cf1c4f565d4f5b3d38ef96dc46e1f95dc55f32

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Konrad Basler
2. G. Hausmann
3. W. Nelson
4. B. Gumbiner
5. F. Orsenigo
6. M. Lampugnani
7. E. Dejana
8. Wenqing Xu

In Molecular Biology

1. Zsuzsanna Dosztányi
2. Konrad Basler
3. G. Hausmann
4. W. Nelson
5. Bálint Mészáros
6. Vladimir N Uversky
7. István Simon
8. E. Dejana

Citations in the corpus

• The E-Cadherin and N-Cadherin Switch in Epithelial-to-Mesenchymal Transition: Signaling, Therapeutic Implications, and Challenges (2019, background): “Protein kinases CK2 and GSK3β could phosphorylate Ser684, Ser686 and Ser692 in the cadherin cytoplasmic domain, which strengthens the E-cadherin/β-catenin complex and cell–cell adhesion, thereby limiting Wnt signaling [146].”
• The role of adherens junctions and VE-cadherin in the control of vascular permeability (2008, background): “In several systems, the tyrosine phosphorylation of β-catenin reduces its affinity for the cadherin cytoplasmic tail and increases its turnover at junctions (Huber and Weis, 2001; Lilien and Balsamo, 2005).”
• β-Catenin hits chromatin: regulation of Wnt target gene activation (2009, background): “The central repeats that span R3–R10 are viewed as the core TCF interaction regio”
• Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development. (2002, background): “The - and -catenins interact with the cadherin cytoplasmic domain in a stretch of sequence of 100 amino acids (200), and -catenin (also an actin-binding protein) links the cadherin to the actin cytoskeleton (177, 235) via its interactions with a number of actin-binding proteins, such as -actinin, vi”
• Prediction of Protein Binding Regions in Disordered Proteins (2009, background): “A few experimentally verified disordered complexes missing from Disprot were added to this set [42,43,62,91–93].”
• Small-molecule antagonists of the oncogenic Tcf/β-catenin protein complex (2004, background): “Recent studies show that other protein-protein interac-sents a potential obstacle in developing selective drugs (Huber and Weis, 2001).”
• Reading protein modifications with interaction domains (2006, background): “However, phosphorylation of multiple Ser residues in an unstructured 15-residue segment of E-cadherin results in novel contacts with β-catenin ( Table 1 ) and a consequent ordering of this region of the E-cadherin tai”
• Deconstructing the cadherin-catenin-actin complex. (2005, background): “The cadherin cytoplasmic domain forms a high affinity , 1:1 complex with b-catenin, and b-catenin binds with lower affinity to a-catenin (Aberle et al., 1994; Hinck et al., 1994; Pokutta and Weis, 2000; Huber and Weis, 2001).”