Abstract
Cadherins are transmembrane adhesion molecules that mediate homotypic cell-cell contact. In adherens junctions, the cytoplasmic domain of cadherins is functionally linked to the actin cytoskeleton through a series of proteins known as catenins. E-cadherin binds to β-catenin, which in turn binds to α-catenin to form a ternary complex. α-Catenin also binds to actin, and it was assumed previously that α-catenin links the cadherin-catenin complex to actin. However, biochemical, structural and live-cell imaging studies of the cadherin-catenin complex and its interaction with actin show that binding of β-catenin to α-catenin prevents the latter from binding to actin. Biochemical and structural data indicate that α-catenin acts as an allosteric protein whose conformation and activity changes depending on whether or not it is bound to β-catenin. Initial contacts between cells occur on dynamic lamellipodia formed by polymerization of branched actin networks, a process controlled by the Arp2/3 (actin-related protein 2/3) complex. α-Catenin can suppress the activity of Arp2/3 by competing for actin filaments. These findings lead to a model for adherens junction formation in which clustering of the cadherin-β-catenin complex recruits high levels of α-catenin that can suppress the Arp2/3 complex, leading to cessation of lamellipodial movement and formation of a stable contact. Thus α-catenin appears to play a central role in cell-cell contact formation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 141-147 |
| Number of pages | 7 |
| Journal | Biochemical Society Transactions |
| Volume | 36 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 2008 |
| Externally published | Yes |
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Keywords
- Actin
- Actin-related protein 2/3 complex (Arp2/3 complex)
- Adherens junction
- Cadherin
- Catenin
- Cell adhesion
ASJC Scopus subject areas
- Biochemistry
Cite this
Biochemical and structural analysis of α-catenin in cell-cell contacts. / Pokutta, Sabine; Drees, Frauke; Yamada, Soichiro; Nelson, W. James; Weis, William I.
In: Biochemical Society Transactions, Vol. 36, No. 2, 04.2008, p. 141-147.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Biochemical and structural analysis of α-catenin in cell-cell contacts
AU - Pokutta, Sabine
AU - Drees, Frauke
AU - Yamada, Soichiro
AU - Nelson, W. James
AU - Weis, William I.
PY - 2008/4
Y1 - 2008/4
N2 - Cadherins are transmembrane adhesion molecules that mediate homotypic cell-cell contact. In adherens junctions, the cytoplasmic domain of cadherins is functionally linked to the actin cytoskeleton through a series of proteins known as catenins. E-cadherin binds to β-catenin, which in turn binds to α-catenin to form a ternary complex. α-Catenin also binds to actin, and it was assumed previously that α-catenin links the cadherin-catenin complex to actin. However, biochemical, structural and live-cell imaging studies of the cadherin-catenin complex and its interaction with actin show that binding of β-catenin to α-catenin prevents the latter from binding to actin. Biochemical and structural data indicate that α-catenin acts as an allosteric protein whose conformation and activity changes depending on whether or not it is bound to β-catenin. Initial contacts between cells occur on dynamic lamellipodia formed by polymerization of branched actin networks, a process controlled by the Arp2/3 (actin-related protein 2/3) complex. α-Catenin can suppress the activity of Arp2/3 by competing for actin filaments. These findings lead to a model for adherens junction formation in which clustering of the cadherin-β-catenin complex recruits high levels of α-catenin that can suppress the Arp2/3 complex, leading to cessation of lamellipodial movement and formation of a stable contact. Thus α-catenin appears to play a central role in cell-cell contact formation.
AB - Cadherins are transmembrane adhesion molecules that mediate homotypic cell-cell contact. In adherens junctions, the cytoplasmic domain of cadherins is functionally linked to the actin cytoskeleton through a series of proteins known as catenins. E-cadherin binds to β-catenin, which in turn binds to α-catenin to form a ternary complex. α-Catenin also binds to actin, and it was assumed previously that α-catenin links the cadherin-catenin complex to actin. However, biochemical, structural and live-cell imaging studies of the cadherin-catenin complex and its interaction with actin show that binding of β-catenin to α-catenin prevents the latter from binding to actin. Biochemical and structural data indicate that α-catenin acts as an allosteric protein whose conformation and activity changes depending on whether or not it is bound to β-catenin. Initial contacts between cells occur on dynamic lamellipodia formed by polymerization of branched actin networks, a process controlled by the Arp2/3 (actin-related protein 2/3) complex. α-Catenin can suppress the activity of Arp2/3 by competing for actin filaments. These findings lead to a model for adherens junction formation in which clustering of the cadherin-β-catenin complex recruits high levels of α-catenin that can suppress the Arp2/3 complex, leading to cessation of lamellipodial movement and formation of a stable contact. Thus α-catenin appears to play a central role in cell-cell contact formation.
KW - Actin
KW - Actin-related protein 2/3 complex (Arp2/3 complex)
KW - Adherens junction
KW - Cadherin
KW - Catenin
KW - Cell adhesion
UR - http://www.scopus.com/inward/record.url?scp=42449102211&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=42449102211&partnerID=8YFLogxK
U2 - 10.1042/BST0360141
DO - 10.1042/BST0360141
M3 - Article
C2 - 18363554
AN - SCOPUS:42449102211
VL - 36
SP - 141
EP - 147
JO - Biochemical Society Transactions
JF - Biochemical Society Transactions
SN - 0300-5127
IS - 2
ER -