| + |
SRC | down-regulates activity 
phosphorylation
|
CDH5 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246462 |
Tyr658 |
GEMDTTSyDVSVLNS |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 16027153 |
cadherins also act to prevent epithelial cell motilityCadherin-cytoskeletal interactions occur through a number of adaptor proteins that interact with the C-terminal portion of the cadherin cytoplasmic tail, including the _-, _-, and _-catenin (6, 10). Additionally, VE-cadherin stability at the plasma membrane may be regulated by the binding of p120-catenin to the juxtamembrane region of the cytoplasmic tailWe show here that tyrosine phosphorylation of the adherens junction protein VE-cadherin at two critical tyrosines, Tyr-658 and Tyr-731, via tyrosine kinase activation or phosphatase inactivation was sufficient to prevent the binding of p120- and beta-catenin, respectively, to the cytoplasmic tail of VE-cadherinVE-cadherin becomes phosphorylated on Tyr-658 and/or Tyr-731 in response to Src kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246466 |
Tyr731 |
PYDTLHIyGYEGSES |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 16027153 |
cadherins also act to prevent epithelial cell motilityCadherin-cytoskeletal interactions occur through a number of adaptor proteins that interact with the C-terminal portion of the cadherin cytoplasmic tail, including the _-, _-, and _-catenin (6, 10). Additionally, VE-cadherin stability at the plasma membrane may be regulated by the binding of p120-catenin to the juxtamembrane region of the cytoplasmic tailWe show here that tyrosine phosphorylation of the adherens junction protein VE-cadherin at two critical tyrosines, Tyr-658 and Tyr-731, via tyrosine kinase activation or phosphatase inactivation was sufficient to prevent the binding of p120- and beta-catenin, respectively, to the cytoplasmic tail of VE-cadherinVE-cadherin becomes phosphorylated on Tyr-658 and/or Tyr-731 in response to Src kinase activity. |
|
| Publications: |
2 |
Organism: |
Cricetulus Griseus |
| + |
SRC | up-regulates 
phosphorylation
|
CDH5 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148818 |
Tyr685 |
LDARPSLyAQVQKPP |
Homo sapiens |
|
| pmid |
sentence |
| 16909109 |
In vitro src assay, the ve-cadherin cytoplasmic domain is directly phosphorylated by purified src as well as the tyrosine residue 685 (tyr)685-containing peptide finally, we found that in a vegf-induced wound-healing assay, cadherin adhesive activity was impaired by src kinase inhibitors.RPSLY(685)aqvq. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
ARVCF | up-regulates quantity by stabilization
binding
|
CDH5 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252129 |
|
|
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 |
| + |
CDH5 | up-regulates activity
binding
|
CTNNB1 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265867 |
|
|
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 |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
CDH5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265845 |
|
|
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 |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH5 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252132 |
|
|
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 |
| + |
ERG | up-regulates quantity by expression
transcriptional regulation
|
CDH5 |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261595 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18195090 |
Erg overexpression resulted in an approximate 1.8-fold transactivation of VE-cadherin promoter activity. Thus, our data indicate that Erg drives constitutive VE-cadherin expression in human ECs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH5 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252126 |
|
|
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 |
| + |
PTPRB | up-regulates activity
dephosphorylation
|
CDH5 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277131 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19015309 |
Because we had shown previously that VE-PTP supports VE-cadherin function when exogenously expressed in transfected cells, we expected it to be expressed at endothelial cell contacts.|Indeed, tyrosine phosphorylation of VE-cadherin is reduced by VE-PTP in COS-7 and CHO cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDH5
- 
- 