| + |
CASTOR1-CASTOR2 arginine binding complex | down-regulates activity 
binding
|
mTORC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281116 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26972053 |
Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASTOR2 | form complex 
binding
|
CASTOR1-CASTOR2 arginine binding complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281110 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26972053 |
Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASTOR1 | form complex
binding
|
CASTOR1-CASTOR2 arginine binding complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281111 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26972053 |
Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
arginine | down-regulates activity
binding
|
CASTOR1-CASTOR2 arginine binding complex |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281112 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26972053 |
Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
CASTOR1-CASTOR2 arginine binding complex