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CYLD inhibits JNK. 24 / 24
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"These results establish a pivotal role for CYLD in controlling Tak1 function and explain how CYLD negatively regulates IKKbeta and JNK."
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"Recent evidence demonstrates that CYLD negatively regulates the c-Jun N-terminal kinase (JNK) signaling pathway, a critical mediator of cell survival."
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"CYLD can suppress the activation of NF-κB or JNK signaling by removing K63-linked polyubiquitin chains from the signaling complex [27–29,40]."
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"CYLD negatively regulates the activation of IKK and JNK, and its expression is markedly upregulated under conditions of RANKL induced osteoclastogenesis [XREF_BIBR]."
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"The loss of CYLD in both primary T cells and the Jurkat T cell line causes the constitutive activation of Tak1 as well as its downstream targets JNK and IKK."
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"CYLD negatively regulates NF-κB, WNT, and JNK signaling, and inactivating mutations can result in aberrant pathway activation, ultimately leading to enhanced cell proliferation, inhibition of apoptosi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"CYLD also negatively regulates the c-Jun N-terminal kinase (JNK) signaling pathway and mitogen activated protein kinase (MAPK) pathway, which are known to participate in a wide range of cellular processes, including proliferation, differentiation, and apoptosis of cholesteatoma [XREF_BIBR, XREF_BIBR]."
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"Expression of a non cleavable form of CYLD inhibited activation of the JNK pathway and expression of AP-1 target genes in a T-cell line, although CYLD silencing only minimally increased JNK activation [XREF_BIBR], possibly because of redundancy with other deubiquitinating enzymes."
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"C-Jun N-terminal kinase (JNK) signaling pathway activated by TNF alpha, anti-CD40 antibody, IL-1 beta, and lipopolysaccharide is repressed by CYLD by reducing the activity of MKK7 and JNKK2, which is [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"CYLD, a de-ubiquitinating enzyme, suppresses both the NF-kappaB pathway [XREF_BIBR, XREF_BIBR] and the c-Jun N-terminal kinase pathway [XREF_BIBR - XREF_BIBR]."
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"Ubiquitination is subject to negative regulation by deubiquitinases (DUBs) such as CYLD which removes K63-Ub and M1-Ub from target proteins, and thereby negatively regulates NF-κB and JNK pathways (4, 5)."
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"Loss of CYLD in T cells leads to constitutive activation of TAK1 and its downstream kinases c-Jun N -terminal kinase (JNK) and IκB kinase β (IKKβ)."
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"Depending on the cellular context CYLD has been shown to negatively regulate NF-kappaB and/or JNK signalling pathways resulting in suppression of cell proliferation and survival."
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"Conversely, loss of the K63 specific deubiquitinase CYLD causes spontaneous activation of IKK and JNK as well as their upstream kinase Tak1."
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"Subsequent studies have demonstrated that CYLD negatively regulates nuclear factor kappa B (NF-kappaB) and c-Jun N-terminal kinase (JNK) pathways, and plays a critical role in immunity, lipid metaboli[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
19800320
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"However, CYLD was also reported to negatively regulate JNK signaling in culture cells ( Reiley et al., 2004 ) and macrophages ( Zhang et al., 2006 )."
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"Thus, CYLD could positively or negatively regulate JNK signaling in a cell-type-specific manner.To genetically map the epistasis of dCYLD and dTRAF2 in the Egr-JNK pathway, we examined the genetic int[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"While CYLD negatively regulates JNK activation by diverse stimuli, it exerts an inhibitory effect on NF-kappaB pathway by anti-CD40, LPS, and IL-1beta."
19800320
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"We show that mesenchymal Cyld contributes to prevent excessive JNK and NF-κB activation in TNF-stimulated naive and arthritic SFs."
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"CYLD deletion causes accumulation of constitutively active TAK1, and its downstream kinases JNK and IKK, which results in T cells that become hyper-responsive to TCR stimulation."
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"On the contrary, CYLD WT overexpression leads to a diminished JNK activation both in non stimulated and in TNF-alpha-stimulated A-CYLD WT cells (XREF_FIG)."
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"CYLD, a tumor suppressor and a target gene of NF-kappaB, negatively regulates NF-kappaB and JNK activation by removing K63 linked polyubiquitin chains from TRAF2 and TRAF6 as well as several other signaling proteins [XREF_BIBR, XREF_BIBR]."
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"However, because Cyld deficiency did not cause the activation of ERK, the target of CYLD might be an intermediate signaling factor specifically mediating the activation of JNK and IKKbeta."
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"Treatment with MPA also increases the transcription of ubiquitin carboxyl-terminal hydrolase CYLD (log2FC 0.12, padj = 0.04), which is known to suppress the NF-κB, p38MAPK and c-Jun N-terminal kinase (JNK) cascades."
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