IndraLab

Statements

CYLD binds STING1. 16 / 16
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"CYLD associates with STING in a ubiquitination-dependent manner."
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"In contrast, the E3 ligase Trim32 or Trim 56 failed to promote the association between STING and CYLD (Fig 4A and 4B)."
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"We found that ubiquitinated STING, but not unmodified STING, interacted with CYLD in vitro , suggesting that CYLD associates with STING in a ubiquitination-dependent manner."
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"Then, the endogenous association between STING and CYLD was further investigated."
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"As shown in xref , unlike RNF5, TRIM29 could not promote CYLD-STING association."
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"Fifth, CYLD associated with STING via the K48-linked polyubiquitin chains on STING, and this association appeared to be enhanced upon HSV-1 infection."
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"HA-tagged STING did not interact with Myc-tagged CYLD."
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"Furthermore, as it was reported that RNF5 ubiquitinated STING at K150 [ xref ], we examined whether lysine 150 of STING could influence the association of STING with CYLD."
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"Interestingly, the association between CYLD and STING was detected only when the E3 ligase RNF5 was coexpressed."
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"Notably, the endogenous interaction between STING and CYLD was substantially enhanced upon HSV-1 infection ( xref )."
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"Therefore, we wondered whether CYLD could interact directly with STING."
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"Notably, the endogenous interaction between STING and CYLD was substantially enhanced upon HSV-1 infection (Fig 4F)."
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"Therefore, we examined if TRIM29 has any effect on the association of STING with CYLD."
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"To further investigate if STING and CYLD interact directly, we performed the indicated experiments in xref ."
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"Moreover, a catalytically dead mutant of RNF5 (C42S) did not promote the interaction between STING and CYLD ( xref )."
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"Taken together, these data establish that CYLD associates with STING in a ubiquitination-dependent manner and colocalizes with STING in the Golgi upon HSV-1 infection."
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