| + |
MUC4 | down-regulates quantity 
binding
|
FBLN2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282708 |
|
|
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 22105367 |
MUC4 is a large transmembrane type I glycoprotein that is overexpressed in pancreatic cancer (PC) and has been shown to be associated with its progression and metastasis. Here we showed that the nidogen-like (NIDO) domain of MUC4, which is similar to the G1-domain present in the nidogen or entactin (an extracellular matrix protein), contributes to the protein-protein interaction property of MUC4.Importantly, the MUC4-NIDO domain interacts with fibulin-2, and this may be a possible mechanism through which MUC4 promotes pancreatic cancer metastasis.In the current study, we postulated that under cancer conditions, through the NIDO-domain, MUC4 present at the basal surface of the epithelial cells may competitively inhibit the normal interaction between fibulin-2 and nidogen protein of the basement membrane (BM) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBLN2 | up-regulates quantity by stabilization 
binding
|
NID1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282710 |
|
|
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 22105367 |
MUC4 is a large transmembrane type I glycoprotein that is overexpressed in pancreatic cancer (PC) and has been shown to be associated with its progression and metastasis. Here we showed that the nidogen-like (NIDO) domain of MUC4, which is similar to the G1-domain present in the nidogen or entactin (an extracellular matrix protein), contributes to the protein-protein interaction property of MUC4.Importantly, the MUC4-NIDO domain interacts with fibulin-2, and this may be a possible mechanism through which MUC4 promotes pancreatic cancer metastasis.In the current study, we postulated that under cancer conditions, through the NIDO-domain, MUC4 present at the basal surface of the epithelial cells may competitively inhibit the normal interaction between fibulin-2 and nidogen protein of the basement membrane (BM) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBLN2 | up-regulates quantity by stabilization
binding
|
FBN1 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282700 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17255108 |
Using a panel of recombinant fibrillin-1 swapped domain and deletion fragments, we demonstrate here that the conserved first hybrid domain in fibrillin-1 is essential for binding to fibulin-2, -4, and -5.Formation of ternary complexes between fibrillin-1, fibulins, and tropoelastin demonstrated that fibulin-2 and -5 but much less fibulin-4, are able to act as molecular adaptors between fibrillin-1 and tropoelastin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBLN2 | up-regulates quantity by stabilization
binding
|
ELN |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282703 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17255108 |
Using a panel of recombinant fibrillin-1 swapped domain and deletion fragments, we demonstrate here that the conserved first hybrid domain in fibrillin-1 is essential for binding to fibulin-2, -4, and -5.Formation of ternary complexes between fibrillin-1, fibulins, and tropoelastin demonstrated that fibulin-2 and -5 but much less fibulin-4, are able to act as molecular adaptors between fibrillin-1 and tropoelastin.However, when fibulin-2 or -5 was added to the binding assay, rF16 strongly interacted with tropoelastin, whereas fibulin-4 only marginally mediated the formation of this ternary complex. These data demonstrate that at least fibulin-2 and -5 can mediate binding of fibrillin-1 to tropoelastin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
FBLN2
- 
- 