Abstract
Epithelial cell-cell junctions, organized by adhesion proteins and the underlying actin cytoskeleton, are considered to be stable structures maintaining the structural integrity of tissues. Contrary to the idea that α-catenin links the adhesion protein E-cadherin through β-catenin to the actin cytoskeleton, in the accompanying paper we report that α-catenin does not bind simultaneously to both E-cadherin-β-catenin and actin filaments. Here we demonstrate that α-catenin exists as a monomer or a homodimer with different binding properties. Monomeric α-catenin binds more strongly to E-cadherin-β-catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that α-catenin is an allosteric protein. Significantly, α-catenin directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments. These results indicate a new role for α-catenin in local regulation of actin assembly and organization at sites of cadherin-mediated cell-cell adhesion.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 903-915 |
| Number of pages | 13 |
| Journal | Cell |
| Volume | 123 |
| Issue number | 5 |
| DOIs | |
| State | Published - Dec 2 2005 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
Cite this
α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-filament assembly. / Drees, Frauke; Pokutta, Sabine; Yamada, Soichiro; Nelson, W. James; Weis, William I.
In: Cell, Vol. 123, No. 5, 02.12.2005, p. 903-915.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-filament assembly
AU - Drees, Frauke
AU - Pokutta, Sabine
AU - Yamada, Soichiro
AU - Nelson, W. James
AU - Weis, William I.
PY - 2005/12/2
Y1 - 2005/12/2
N2 - Epithelial cell-cell junctions, organized by adhesion proteins and the underlying actin cytoskeleton, are considered to be stable structures maintaining the structural integrity of tissues. Contrary to the idea that α-catenin links the adhesion protein E-cadherin through β-catenin to the actin cytoskeleton, in the accompanying paper we report that α-catenin does not bind simultaneously to both E-cadherin-β-catenin and actin filaments. Here we demonstrate that α-catenin exists as a monomer or a homodimer with different binding properties. Monomeric α-catenin binds more strongly to E-cadherin-β-catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that α-catenin is an allosteric protein. Significantly, α-catenin directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments. These results indicate a new role for α-catenin in local regulation of actin assembly and organization at sites of cadherin-mediated cell-cell adhesion.
AB - Epithelial cell-cell junctions, organized by adhesion proteins and the underlying actin cytoskeleton, are considered to be stable structures maintaining the structural integrity of tissues. Contrary to the idea that α-catenin links the adhesion protein E-cadherin through β-catenin to the actin cytoskeleton, in the accompanying paper we report that α-catenin does not bind simultaneously to both E-cadherin-β-catenin and actin filaments. Here we demonstrate that α-catenin exists as a monomer or a homodimer with different binding properties. Monomeric α-catenin binds more strongly to E-cadherin-β-catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that α-catenin is an allosteric protein. Significantly, α-catenin directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments. These results indicate a new role for α-catenin in local regulation of actin assembly and organization at sites of cadherin-mediated cell-cell adhesion.
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UR - http://www.scopus.com/inward/citedby.url?scp=28344439885&partnerID=8YFLogxK
U2 - 10.1016/j.cell.2005.09.021
DO - 10.1016/j.cell.2005.09.021
M3 - Article
C2 - 16325583
AN - SCOPUS:28344439885
VL - 123
SP - 903
EP - 915
JO - Cell
JF - Cell
SN - 0092-8674
IS - 5
ER -