IndraLab

Statements


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No evidence text available

reach
"OTUB1 specifically interacts with DEPTOR via its N-terminal domain, removes the Ub chain on DEPTOR and stabilizes DEPTOR via DUB activity in an Asp88 dependent but not Cys91 dependent manner."

sparser
"We found that OTUB1 directly interacted with DEPTOR via its N-terminal domain, deubiquitinated DEPTOR, and thereby stabilized DEPTOR in a Cys-91-independent but Asp-88-dependent manner, suggesting that OTUB1 targets DEPTOR for deubiquitination via a deubiquitinase activity-independent non-canonical mechanism."

sparser
"The interaction between OTUB1 and DEPTOR was enhanced when the cells were treated with amino acids."

reach
"OTUB1 can directly bind to DEPTOR through the N-terminal domain, which can thereby enable the deubiquitination of DEPTOR, increasing the DEPTOR expression level and inhibiting the activity of mTORC1 (Zhao et al., 2018)."

sparser
"Lysine ubiquitination by SidC and SdcA promotes interactions between OTUB1 and DEPTOR, an inhibitor of the MTORC1 pathway, thus suppressing MTORC1 signaling."

No evidence text available

sparser
"OTUB1 can directly bind to DEPTOR through the N-terminal domain, which can thereby enable the deubiquitination of DEPTOR, increasing the DEPTOR expression level and inhibiting the activity of mTORC1 ( xref )."

sparser
"OTUB1 specifically interacts with DEPTOR via its N-terminal domain, removes the Ub chain on DEPTOR and stabilizes DEPTOR via DUB activity in an Asp88-dependent but not Cys91-dependent manner (Fig. xref )."

reach
"We found that OTUB1 directly interacted with DEPTOR via its N-terminal domain, deubiquitinated DEPTOR, and thereby stabilized DEPTOR in a Cys-91-independent but Asp-88-dependent manner, suggesting that OTUB1 targets DEPTOR for deubiquitination via a deubiquitinase activity independent non canonical mechanism."

reach
"The interaction between OTUB1 and DEPTOR was enhanced when the cells were treated with amino acids."