Deconstructing the cadherin-catenin-actin complex.

By Soichiro Yamada, S. Pokutta, Frauke Drees, William I. Weis, W. Nelson. Cell, 2005

1,060 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/07b4f61eb776b00811f743e7eb9766bfebc28239

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. M. Takeichi
2. Wenxiang Meng
3. Konrad Basler
4. G. Hausmann
5. T. Valenta
6. W. Nelson
7. C. Niessen
8. T. Harris

In Molecular Biology

1. T. Valenta
2. Konrad Basler
3. G. Hausmann
4. M. Takeichi
5. Wenxiang Meng
6. W. Nelson
7. C. Niessen
8. T. Harris

Citations in the corpus

• The many faces and functions of β‐catenin (2012, positive): “Consequently, the binding of a -catenin to the cadherin– b -catenin complex negatively regulates its activity on actin polymerization (Yamada et al , 2005).”
• Phospho-regulation of β-Catenin Adhesion and Signaling Functions (2007, background): “24,67), β-catenin binding to cadherin remains a prerequisite for adhesion due to its role in protecting the cadherin cytoplasmic domain from rapid degradation (40), enhancing the efficiency of endoplasmic reticulum to cell surface transport (10) and recruiting α-catenin to sites of cell-cell contact”
• Cell surface mechanics and the control of cell shape, tissue patterns and morphogenesis (2007, background): “Recent work has emphasized the fact that adhesion does not simply rely on cadherin interactions but also, and most importantly, on the dynamic interactions with cortical actin and on actin organization per se”
• Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. (2008, background): “Conversely, homo-dimeric α-catenin binds actin filaments but not β-catenin [70]; α-catenin homo-dimer binding to actin also appears to compete binding of the Arp2/3 complex to actin filaments thereby suppressing actin polymerization [72].”
• Tight Junction Pore and Leak Pathways: A Dynamic Duo (2011, background): “One possible explanation of these data is that occludin and ZO-1 diffuse within the membrane bound to one another, as has been suggested for the E-cadherin-β-catenin complex (130).”
• Wnt signaling: is the party in the nucleus? (2006, background): “Although it had been assumed that the adhesion complexes are anchored to actin through -catenin, recent studies show that the -catenin:actin complexes interact only transiently, if at all, with the membrane-anchored E-cadherin junctional complexes (Drees et al. 2005; Yamada et al. 2005).”
• Listeria monocytogenes: a multifaceted model (2006, background): “As was recently shown, α-catenin cannot simultaneously interact with actin filaments and the E-cadherin–β-catenin complex, indicating that α-catenin is not an actin anchor but is, instead, an actin-filament organize”
• Tight junctions/adherens junctions: basic structure and function. (2007, background): “However, recent studies from the Nelson and Weis groups found no in vitro evidence for the existence of a ternary cadherin-b – a -catenin–actin complex (Yamada et al ., 2005).”
• Cadherins in development: cell adhesion, sorting, and tissue morphogenesis. (2006, background): “However, it was recently shown using a combination of direct binding studies with purified proteins and measurement of protein dynamics in live cells that -catenin does not interact with -catenin and filamentous actin simultaneously (Drees et al. 2005; Yamada et al. 2005).”