| + |
mTORC2 | up-regulates quantity by stabilization 
phosphorylation
|
FBXW8 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271940 |
Ser85 |
DVASRSRsPLAREGA |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23142081 |
MTORC2 stabilizes Fbw8 by phosphorylation at Ser86 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FBXW8 | up-regulates activity
binding
|
Cullin 7-RBX1-Skp1 |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271631 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1. We next investigated whether in vitro ubiquitination of cyclin D1 through the SCF-like (SCFL) complex FBXW8 (SKP1-CUL7-FBXW8-RBX1/SCFLFBXW8) requires phosphorylation of cyclin D1 at Thr286 (Fig. 3F). Polyubiquitination through SCFLFBXW8 was dramatically reduced by the depletion of ERK2 (lane 2). Furthermore, cyclin D1 polyubiquitination was largely prevented by the alanine-for-Thr286 substitution (T286A, lane 3), suggesting that phosphorylation of cyclin D1 at Thr286 is necessary for ubiquitination by SCFLFBXW8. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271942 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23142081 |
Defective IRS-1 degradation was due to attenuated expression and phosphorylation of the ubiquitin ligase substrate-targeting subunit, Fbw8. mTORC2 stabilizes Fbw8 by phosphorylation at Ser86, allowing the insulin-induced translocation of Fbw8 to the cytosol where it mediates IRS-1 degradation. We provide evidence that mTORC2 can stabilize Fbw8, the substrate-targeting subunit of the CUL7 E3 ligase complex that has been shown to mediate degradation of IRS-1 . |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
FBXW8 | down-regulates quantity by destabilization 
binding
|
CCND1 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271624 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
We next investigated whether in vitro ubiquitination of cyclin D1 through the SCF-like (SCFL) complex FBXW8 (SKP1-CUL7-FBXW8-RBX1/SCFLFBXW8) requires phosphorylation of cyclin D1 at Thr286 (Fig. 3F). Polyubiquitination through SCFLFBXW8 was dramatically reduced by the depletion of ERK2 (lane 2). Furthermore, cyclin D1 polyubiquitination was largely prevented by the alanine-for-Thr286 substitution (T286A, lane 3), suggesting that phosphorylation of cyclin D1 at Thr286 is necessary for ubiquitination by SCFLFBXW8. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW8 | up-regulates activity
binding
|
Cullin 1-RBX1-Skp1 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271632 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1. We next investigated whether in vitro ubiquitination of cyclin D1 through the SCF-like (SCFL) complex FBXW8 (SKP1-CUL7-FBXW8-RBX1/SCFLFBXW8) requires phosphorylation of cyclin D1 at Thr286 (Fig. 3F). Polyubiquitination through SCFLFBXW8 was dramatically reduced by the depletion of ERK2 (lane 2). Furthermore, cyclin D1 polyubiquitination was largely prevented by the alanine-for-Thr286 substitution (T286A, lane 3), suggesting that phosphorylation of cyclin D1 at Thr286 is necessary for ubiquitination by SCFLFBXW8. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW8 | down-regulates quantity by destabilization
binding
|
IRS1 |
0.477 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271939 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23142081 |
Defective IRS-1 degradation was due to attenuated expression and phosphorylation of the ubiquitin ligase substrate-targeting subunit, Fbw8. mTORC2 stabilizes Fbw8 by phosphorylation at Ser86, allowing the insulin-induced translocation of Fbw8 to the cytosol where it mediates IRS-1 degradation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
FBXW8
- 
- 