IndraLab

Statements


| 5 6

sparser
"USP20 can bind, de-ubiquitinate and stabilize ULK1 at a basal level and plays an important role in autophagy initiation."

reach
"USP20 interacts with and deubiquitinates ULK1, thus protecting it from degradation."

reach
"However, the interaction between ULK1 and USP20 is weakened upon prolonged induction of autophagy (4 to 8 h), leading to a reduction of the level of ULK1 protein while its ubiquitinated form accumulates [XREF_BIBR]."

sparser
"However, the interaction between ULK1 and USP20 is weakened upon prolonged induction of autophagy (4 to 8 h), leading to a reduction of the level of ULK1 protein while its ubiquitinated form accumulates [64]."

reach
"Under prolonged starvation, the binding of USP20 to ULK1 is diminished, leading to autophagy inhibition [43]."

sparser
"Under prolonged starvation, the binding of USP20 to ULK1 is diminished, leading to autophagy inhibition [ xref ]."

reach
"At basal state, USP20 binds to and stabilizes ULK1 by removing the ubiquitin moiety, thereby interfering with the lysosomal degradation of ULK1."

sparser
"However, the interaction between ULK1 and USP20 is weakened upon prolonged induction of autophagy (4 to 8 h), leading to a reduction of the level of ULK1 protein while its ubiquitinated form accumulates [ xref ]."

sparser
"During prolonged starvation, NEDD4L catalyzes the K27 and K29 ubiquitination on ULK1 [ xref ], whereas the interaction between USP20 and ULK1 is attenuated [ xref ]."

reach
"During prolonged starvation, NEDD4L catalyzes the K27 and K29 ubiquitination on ULK1 [58], whereas the interaction between USP20 and ULK1 is attenuated [43]."

sparser
"In prolonged starvation, the interaction between USP20 and ULK1 reduces to terminate autophagy [ xref ]."
| PMC