IndraLab

Statements

OTUB1 is phosphorylated on S16. 23 / 23
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"We set out to characterize the phosphorylation of OTUB1 at Ser 16 and Ser 18 in vitro and in vivo."
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"However, phosphorylation of OTUB1 at serine 16 (S16) was unchanged in SHP2 siRNA-treated cells (Fig. xref )."
37330581
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"Additionally, we assessed the effects of OTUB1 phosphorylation at Ser16 on p27 expression."
38664499
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"Pharmacological inhibition or genetic ablation of CK2 blocked the phosphorylation of OTUB1 at Ser 16 and its nuclear localization in various cells."
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"The phosphorylation of OTUB1 at Ser 16 did not alter its catalytic activity in vitro, its ability to bind K63-linked ubiquitin chains in vitro and its ability to interact with the E2 enzyme UBE2N in vitro."
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"To test whether OTUB1 is a bona fide substrate of CK2 in cells, the phosphorylation of OTUB1 at Ser 16 was further investigated by using pharmacological and genetic tools to inhibit CK2 in HEK293 cells."
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"Treatment of cells with TDB decreased the phosphorylation of endogenous OTUB1 at Ser 16 to below detection in comparison to amount observed under control conditions by immunoblotting ( xref )."
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"Furthermore, quinalizarin, an inhibitor of CK2 that does not target PIM1 or DYRK1A ( xref ), also inhibited the phosphorylation of endogenous OTUB1 at Ser 16 ( xref )."
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"Its subcellular location is regulated by casein kinase 2 (CK2), which phosphorylates Ser16 of OTUB1 moving it from the cytoplasm to the nucleus [ xref ]."
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"To further confirm that CK2 was the mediator for OTUB1 Ser 16 phosphorylation in cells, a loss-of-function experiment was employed."
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"Two CK2 siRNAs ( #1 and #3) that yielded a robust CK2 knockdown both resulted in the depletion of Ser 16 phosphorylation of HA-OTUB1 in HEK293 cells ( xref )."
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"Phosphorylation of OTUB1 at Ser 16 does not affect its catalytic activity and interactions with UBE2N."
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"Here, we investigated whether CK2 mediated the phosphorylation of OTUB1 at Ser 16 and what functional relevance this modification had in various cell types."
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"Deubiquitylation was observed in the absence and presence of UBE2D2 and the phosphorylation of OTUB1 at Ser 16 did not substantially alter its catalytic activity ( xref )."
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"We tested whether the phosphorylation of OTUB1 at Ser 16 , which alters its subcellular localization, was essential for the ability of OTUB1 to modulate IR-induced DNA damage repair."
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"Consistent with this notion, treatment of U2OS cells with TDB, which inhibited the phosphorylation of OTUB1 at Ser 16 and caused its nuclear exclusion, also impaired 53BP1 foci formation upon IR irradiation ( xref )."
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"Our findings show that the phosphorylation of OTUB1 at Ser 16 did not impact its catalytic activity and its ability to interact with K63-linked ubiquitin chains as well as the E2 enzyme, UBE2N. Instead, we demonstrated that Ser 16 phosphorylation of OTUB1 was essential for its nuclear accumulation, suggesting that nuclear roles of OTUB1 are likely to be regulated through CK2-mediated phosphorylation of OTUB1."
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"For example, the phosphorylation of OTUB1 at Ser16 site leads to its nuclear localization, which is very important to repair DNA damage [ 31 ]."
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"The observation that the phosphorylation of OTUB1 at Ser 16 induced its nuclear accumulation suggests that its subcellular localization is regulated through phosphorylation."
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"Casein kinase 2 triggers OTUB1 nuclear localization by phosphorylating OTUB1 at Ser 16 ( xref )."
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No evidence text available
18669648
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"For example, the phosphorylation of OTUB1 at Ser 16 and Ser 18 , by unknown kinases, promotes cellular susceptibility to Yersinia enterocolitica and pseudotuberculosis infection ( xref )."
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"Here, we found that the phosphorylation of OTUB1 at Ser 16 and its subsequent nuclear accumulation is mediated by casein kinase 2 (CK2)."
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