+ |
KLHL8 | down-regulates quantity by destabilization
binding
|
RAPSN |
0.496 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271781 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
19158078 |
We found that rapsyn was polyubiquitinated by KLHL8-containing E3 ligase, but not by KEAP1-containing E3 ligase, clearly indicating that rapsyn is a direct substrate of KLHL8-containing E3 ligase in mammals. We next examined the effect of KLHL-8 depletion on the ubiquitination of rapsyn by performing RNAi experiments in mammalian cells. We found that knockdown of KLHL8 in 3T3 cells reduced the level of rapsyn ubiquitination (Fig. 5C), again indicating that the maintenance mechanism for rapsyn stability is conserved in mammals.The in vitro ubiquitination of mammalian rapsyn by CUL3-containing E3 ligase and the effect of KLHL8 knockdown on the ubiquitination of rapsyn. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
KLHL8 | up-regulates activity
binding
|
Cullin 3-RBX1-Skp1 |
0.412 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271783 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
19158078 |
We found that rapsyn was polyubiquitinated by KLHL8-containing E3 ligase, but not by KEAP1-containing E3 ligase, clearly indicating that rapsyn is a direct substrate of KLHL8-containing E3 ligase in mammals. We next examined the effect of KLHL-8 depletion on the ubiquitination of rapsyn by performing RNAi experiments in mammalian cells. We found that knockdown of KLHL8 in 3T3 cells reduced the level of rapsyn ubiquitination (Fig. 5C), again indicating that the maintenance mechanism for rapsyn stability is conserved in mammals.The in vitro ubiquitination of mammalian rapsyn by CUL3-containing E3 ligase and the effect of KLHL8 knockdown on the ubiquitination of rapsyn. |
|
Publications: |
1 |
Organism: |
Mus Musculus |