| + |
HSP90AA1 | up-regulates quantity by stabilization 
binding
|
FLCN |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256505 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
Here we show that the stability of the tumour suppressor folliculin (FLCN) depends on the chaperone function of Hsp90. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSPA1A | up-regulates quantity by stabilization
binding
|
FLCN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256506 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
These data suggest that inhibition of Hsp70 does not lead to an increase in misfolded FLCN but instead to its degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSP90AB1 | up-regulates quantity by stabilization
binding
|
FLCN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261417 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 function as co-chaperones. FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261418 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 function as co-chaperones. FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FLCN | up-regulates activity
gtpase-activating protein
|
RRAGC |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256503 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24095279 |
The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1 [..} RagC/D is a key regulator of the interaction of mTORC1 with the Rag heterodimer and that, unexpectedly, RagC/D must be GDP-bound for the interaction to occur |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLCN | up-regulates activity
gtpase-activating protein
|
RRAGD |
0.676 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256504 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24095279 |
The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1 [..} RagC/D is a key regulator of the interaction of mTORC1 with the Rag heterodimer and that, unexpectedly, RagC/D must be GDP-bound for the interaction to occur |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FLCN
- 
- 