IndraLab

Statements

OTUD4 is phosphorylated. 14 / 14
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"Studies have confirmed that casein kinase II (CK2) induces the phosphorylation of OTUD4 at residues Ser202, which is adjacent to the catalytic OTU domain ( xref )."
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"This activity depends on the phosphorylation of OTUD4 near its catalytic domain ( xref ) as well as a putative UIM motif adjacent to the OTU domain ( xref )."
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"In this study, we show that OTUD4, a K48-specific deubiquitinase which we previously showed to be important for maintaining the stability of alkylation repair enzymes ( xref ), has a completely distinct function in modulating innate immune signaling via NF-κB. We find that OTUD4 is phosphorylated in vivo , activating an unrecognized K63-linked deubiquitinase activity."
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"Knockdown of the kinase CK2α or CK2α prime, or both in HEK293 cells decreased phosphorylation of purified OTUD4, and similarly impaired OTUD4 K63 DUB activity ( xref and xref )."
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"In contrast, the phosphorylation of OTUD4 occurs at a SXXE/D motif xref which is recognised by the kinase casein kinase 2 (CK2) xref , xref ."
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"Furthermore, CKII-induced phosphorylation of OTUD4 promoted the preferential hydrolysis of the Ub chain changed from K48- to K63-linked chains, which plays an essential role in innate immune signalling ( xref )."
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"Zhao et al. demonstrate that OTUD4 is phosphorylated near its catalytic domain, activating a dormant K63-specific deubiquitinase activity."
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"Whether or not OTUD4 is also phosphorylated when acting in these different compartments requires further investigation."
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"Recent evidence however, has revealed that phosphorylation of OTUD4 can alter the enzymatic activity of the protein, permitting a K63-linkage specific deubiquitination of the Toll like receptor/ Interleukin-1 receptor (TLR/IL-1R) associated factor, MyD88 xref ."
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"In addition, phosphorylation of OTUD4 confers K63 deubiquitinase activity, allowing it to deubiquitinate MyD88 and subsequently deactivate TLR-mediated NF-κB signaling [ xref ]."
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"Since OTUD4 appears to regulate MyD88-dependent signaling, we wished to determine whether phosphorylation of OTUD4 is altered during pathway activation."
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"The phosphorylation of OTUD4, as well its putative UIM motif, are also important for MyD88 deubiquitination ( xref ), and consistently, these features are also critical for regulating IL-1β signaling ( xref )."
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"Here, we demonstrate that the deubiquitinase OTUD4, which nominally encodes a K48-specific deubiquitinase, is phosphorylated near its catalytic domain, activating a latent K63-specific deubiquitinase."
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"Phosphorylation of OTUD4 controls its K63 deubiquitinase activity."
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