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Statements


CYLD ubiquitinates TRAF2. 11 / 12
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"CYLD can inhibit NF-kappaB activity by deubiquitinating and inactivating TRAF2 and TRAF6, RIP, NEMO, and the NF-kappaB co-activator BCL-3."

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"We show that CYLD binds to the NEMO (also known as IKKgamma) component of the IkappaB kinase (IKK) complex, and appears to regulate its activity through de-ubiquitination of TRAF2, as TRAF2 ubiquitination can be modulated by CYLD."

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"Ubiquitination of TRAF2 by CYLD was found to be nearly abolished in the presence of a dominant negative ubiquitin-specific protease mutant deficient in CYLD ( xref )."

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"In immune signaling, CYLD negatively regulates NF-κB by deubiquitinating TRAF2, TRAF6, TAK1, and NEMO (29–32)."

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"CYLD knockdown by siRNA results in constitutive ubiquitination of TRAF2."

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"CYLD mediated regulation of the JNK signaling pathway appears to target TRAF2 ubiquitylation, as CYLD knockdown increases both TRAF2 ubiquitylation and JNK activation, further enhancing cell survival [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"A20 also suppresses necroptosis by deubiquitinating RIPK3 at K5, whereas CYLD mediates necroptotic effects by deubiquitinating TNF receptor associated factor 2 (TRAF2)."

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"Ubiquitination of TRAF2 by CYLD was found to be nearly abolished in the presence of a dominant negative ubiquitin specific protease mutant deficient in CYLD."

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"CYLD binds to the NEMO (also known as IKKg) component of the IkB kinase (IKK) complex and appears to regulate its activity through de-ubiquitination of TRAF2, since the ubiquitination of TRAF2 can be [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"A series of recent reports have shown that CYLD blocks signal transmission through the classical NF-κB cascade by deubiquitinating the TNF receptor-associated factor 2 (TRAF2), TRAF6, and IKK-γ (NEMO)[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"CYLD also decreased IFN promotor activation by deubiquitinating TRAF2 and TRAF6 in HEK293T cells, respectively [XREF_BIBR, XREF_BIBR]."