IndraLab

Statements


CYLD deubiquitinates DDX58. 9 / 9
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"CYLD (cylindromatosis) deubiquitinates RIG-I and several downstream molecules to prevent premature RIG-I activation in uninfected cells [17], while USP3 deubiquitinates RIG-I specifically after viral infection, likely serving as a negative feedback regulator [18]."

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"ORF64, USP25, USP21, USP15, USP3, Cylindromatosis (CYLD), porcine epidemic diarrhea virus papain-like protease 2 (PEDV PLP2) and transmissible gastroenteritis virus papain-like protease1 (TGEV PL1) are the DUBs found to deubiquitinate RIG-I."

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"CYLD (cylindromatosis) deubiquitinates RIG-I and several downstream molecules to prevent premature RIG-I activation in uninfected cells [XREF_BIBR], while USP3 deubiquitinates RIG-I specifically after viral infection, likely serving as a negative feedback regulator [XREF_BIBR]."

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"Tumor suppressor protein cylindromatosis (CYLD) reduced the baseline Lys63-linked ubiquitination of RIG-I in uninfected cells [69]."

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"CYLD can inhibit ubiquitination of the RIG1 cytoplasmic viral RNA sensor and also downregulate antiviral Interferon production by controlling IKK activation [XREF_BIBR]."

"SDC4 likely promotes redistribution of RIG-I and CYLD in a perinuclear pattern post viral infection, and thus enhances the RIG-I-CYLD interaction and potentiates the K63-linked deubiquitination of RIG-I."

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"XREF_BIBR, XREF_BIBR We and others have recently shown that RIG-I ubiquitination and TBK1 and IKKepsilon activation are negatively regulated by CYLD, XREF_BIBR, XREF_BIBR a deubiquitinase known to digest K63 linked ubiquitin chains."

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"CYLD has been shown to deubiquitinate, or prevent ubiquitination of RIG-I in cells."

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"A simple explanation for this result is that the carboxyl-terminal fragment of SDC4 brings RIG-I and CYLD close together, which promotes the deubiquitination of RIG-I by CYLD."