+ |
ARVCF | up-regulates quantity by stabilization
binding
|
CDH3 |
0.333 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252127 |
|
|
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
calcium(2+) | up-regulates activity
chemical activation
|
CDH3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265843 |
|
|
Homo sapiens |
|
pmid |
sentence |
22535893 |
Cadherins are Ca(2+)-dependent cell-cell adhesion molecules that play critical roles in animal morphogenesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH3 |
0.742 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252124 |
|
|
Homo sapiens |
HUAEC Cell |
pmid |
sentence |
14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH3 |
0.298 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252130 |
|
|
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDH3 | up-regulates activity
binding
|
CTNNB1 |
0.845 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265865 |
|
|
Homo sapiens |
|
pmid |
sentence |
21255999 |
At its C-terminus, cadherin interacts with β-catenin, which dynamically associates with α-catenin, a direct binding partner of filamentous actin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |