IndraLab

Statements

RIPK2 binds CYLD. 7 / 7
| 4 3
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"Catalytically inactive CYLD interacted with RIPK2 but failed to reduce K63 ubiquitination of RIPK2 (Figure xref B)."
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"WB analysis of immunoprecipitates detected CYLD and RIPK2 only in WT BMDM but not in Cyld −/− BMDM indicating that CYLD interacts with RIPK2 (Figure xref A)."
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"The crucial importance of the CYLD and RIPK2 interaction for the reduction of protective anti-Lm immune responses is shown by the complete abolishment of the protective effect of Cyld deficiency by RIPK2 inhibition."
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"During in vitro infection of mouse bone marrow derived macrophages (BMDMs) with L. monocytogenes, CYLD binds and deubiquitylates RIPK2, resulting in decreased activation of NF-kappaB and ERK1/2 signaling."
| PMC
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"Here, we demonstrate that CYLD also directly binds to RIPK2 and cleaves K63-polyubiquitin chains from RIPK2 in Lm-infected macrophages resulting in a reduced activation of NF-κB, p38 MAPK, and ERK1/2 and, consequently, in an impaired control of Lm in macrophages."
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"Here, we demonstrate that CYLD also directly binds to RIPK2 and cleaves K63-polyubiquitin chains from RIPK2 in Lm infected macrophages resulting in a reduced activation of NF-kappaB, p38 MAPK, and ERK1/2 and, consequently, in an impaired control of Lm in macrophages."
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reach
"WB analysis of immunoprecipitates detected CYLD and RIPK2 only in WT BMDM but not in Cyld -/- BMDM indicating that CYLD interacts with RIPK2."
26834734