IndraLab

Statements

OTUB1 is hydroxylated on N22. 14 / 14
| 14
sparser
"Ongoing studies are investigating whether hydroxylation of wild-type OTUB1 at N22 impacts on its (non-)canonical activity."
26752685
sparser
"OTUB1 hydroxylation on Asn22 alters its binding behavior, especially with respect to proteins important in metabolic pathways."
27663420
sparser
"Interestingly, OTUB1 Asn22 hydroxylation does not necessarily change its protein stability, which further indicates that not all hydroxylation modifications lead to changes in protein stability."
27663420
sparser
"For example, when OTUB1 is hydroxylated at the Asn22 residue by factor inhibiting HIF (FIH), the interactome and substrates of OTUB1 are elevated, particularly its interaction with metabolism-associated proteins."
34177595
sparser
"In order to investigate if the observed OTUB1 N22 hydroxylation was regulated by physiologically relevant changes in the cellular microenvironment, we incubated HEK293 cells overexpressing both OTUB1 and FIH in 0.2% oxygen for 8 h with and without subsequent re-oxygenation at 21% oxygen for one additional hour."
26752685
sparser
"The analysis of the OTUB1 N22 hydroxylation levels by mass spectrometry showed a significant reduction of OTUB1 N22 hydroxylation in hypoxia which was significantly reversed by re-oxygenation ( xref )."
26752685
sparser
"Nutrient starvation for 8 h with and without re-introduction of nutrients following for one additional hour also down-regulated OTUB1 N22 hydroxylation, although to a lesser degree than hypoxia ( xref )."
26752685
sparser
"We next investigated whether OTUB1 hydroxylation on N22 is FIH-dependent."
26752685
sparser
"Expanding on their previous finding that OTUB1 is hydroxylated ( xref ), Scholz and colleagues determined the factor inhibiting HIF hydroxylates OTUB1 at N22 and that this restricts the OTUB1 interactome ( xref )."
30400005
sparser
"We next investigated possible functional consequences of OTUB1 hydroxylation on N22."
26752685
sparser
"Based on these data, we hypothesize that hydroxylation of N22 on OTUB1 profoundly alters its interaction with other proteins and is therefore likely of functional consequence."
26752685
sparser
"OTUB1 N22 Hydroxylation Does Not Affect its Protein Stability."
26752685
sparser
"We next investigated the impact of the hydroxylation of N22 on the OTUB1 protein."
26752685
sparser
"Overall, these data demonstrate that the hydroxylation of OTUB1 at N22 does not impact on OTUB1 protein stability."
26752685