IndraLab

Statements


USP28 is sumoylated. 17 / 17
| 17

sparser
"To investigate the impact of USP28 SUMOylation on HIF-1α, we generated Flag-USP28 K99R mutant plasmid."

sparser
"We found that USP28 is SUMOylated in normoxia but rapidly deSUMOylated under hypoxia condition."

sparser
"The explicit interactions between SENP1 and USP28 prompted us to further examine whether SENP1 could be a deSUMOylation enzyme for USP28 SUMOylation."

sparser
"Do other post-translational modifications, such as SUMOylation of USP28 or methylation of 53BP1, or multimerization of USP28 or 53BP1, regulate the MSP ( xref ; xref )?"

sparser
"SUMO2-conjugated exogenous USP28 was pulled down by Ni + beads under denaturing conditions, and SUMOylated USP28 protein was detected by anti-Flag antibody."

sparser
"Meanwhile, SENP1 KD HCT116 cells showed increased SUMOylated USP28 when compared with SENP1 WT cells (Fig.  xref b), and overexpression of SENP1 WT, but not SENP1 CA, further increased HIF-1α abundance in the presence of USP28 (Fig.  xref a)."

sparser
"N-terminal sumoylation of USP28 decreases its enzymatic activity [ xref , xref ]."
| PMC

sparser
"Our data display that hypoxia modulates the activity of USP28, which leads to the question whether hypoxia also regulates USP28 SUMOylation."

sparser
"N-terminal SUMOylation of USP28 decreases its enzymatic activity."

sparser
"A study determined that SUMOylation of USP28 usually occurs at lysine 99, which is in the UIM domain of the USP28 N-terminus."

sparser
"We found that without HIF-1α, the SUMOylation of USP28 was increased (Fig.  xref d)."

sparser
"293T cells were co-transfected with HIF-1α, HRE-driven luciferase with renilla as an internal control, and Flag-tagged vector control, Flag-tagged USP28 WT or Flag-tagged USP28 K99R. Our co-transfection data found that the highest HIF-1α luciferase activity was achieved in USP28 K99R transfection group (Fig.  xref b), suggesting that USP28 SUMOylation regulates the transcriptional activity of HIF-1α."

sparser
"Additionally, similar to deubiquitination induced by USP28, SUMOylation of USP28 can be revised by SUMO-specific proteases (SENPs), and expression of SENP1 can be induced by the USP28 substrate HIF-1α [ xref , xref ]."

sparser
"In the present study, we proved that USP28 was SUMOylated under normoxic condition but rapidly deSUMOylated during hypoxia."

sparser
"SUMOylation of USP28 impaired its deubiquitinating activity on HIF-1α."

sparser
"There are no data regarding USP28 sumoylation, but it is possible that USP25 is not the only ubiquitin-specific protease regulated by alternative SUMO or ubiquitin modifications."

sparser
"USP28 SUMOylation regulates its deubiquitinating activity against HIF-1α."