IndraLab

Statements


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"Perhaps because the levels of CYLD and the binding of CYLD to TRAF6 were already reduced following LPA stimulation, we only observed a reduction of this association by TRIP6 overexpression in unstimulated cells."

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"SPIO, HA and SPIO@15HA could notably suppress marker genes expression during osteoclastogenesis stimulated by RANKL and M-CSF (Fig. 7A), showing the capability to inhibit osteoclast differentiation.In our previous work, we have found that clinically used SPIOs can increase p62 expression though TLR4 activation [37], thus induce recruitment of CYLD to inhibited TRAF6 ubiquitination, leading to suppression of RANKL induced signal transduction for osteoclast differentiation [30]."

No evidence text available

sparser
"Given that TRAF6 interacts with CYLD in some cells ( xref , xref ), it is possible that CYLD recruitment was mediated by the initial interaction with TRAF6."

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"For example, the adaptor protein p62, which is required for CYLD binding to TRAF6, regulates the DUB activity of CYLD by promoting CYLD ubiquitination [XREF_BIBR]."

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"Furthermore, mice carrying the p62 and SQSTM1-P 392L mutation show loss of binding between CYLD and TRAF6, and loss of deubiquitination activity of CYLD towards TRAF6, supporting the critical role of CYLD in osteoclast differentiation."

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"However, it is unknown whether there is a direct interaction between CYLD and TRAF-6, and if so, how CYLD regulates TRAF signaling."

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"These results show that CYLD is indeed physically associated with TRAF-6."

sparser
"Perhaps because U373-MG cells expressed very low levels of CYLD, we could barely detect the association of TRAF6 with CYLD even when TRIP6 was depleted."

sparser
"Next, we explored the physical relevance of this TRAF-6-CYLD interaction."

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"CYLD binding to one of its targets, TRAF6, requires the adaptor protein p62, which promotes the deubiquitylation of TRAF6 by CYLD xref and probably also modulates the DUB activity of CYLD through induction of CYLD ubiquitylation xref ."

No evidence text available

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"Protein p62 promotes the binding of CYLD to TRAF6 [XREF_BIBR], a de-ubiquitinating enzyme (DUB) that negatively regulates NF-kappaB activity by reducing TRAF6 auto-ubiquitination [XREF_BIBR]."

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"The data showed that CYLD bound to TRAF6 constitutively, but this interaction was gradually diminished following prolonged LPA stimulation ( xref )."

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"However, it is unknown whether there is a direct interaction between CYLD and TRAF-6, and if so, how CYLD regulates TRAF signaling."

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"TRIP6 also attenuates the association of CYLD with TRAF6 in unstimulated HEK293T cells, although the effect is much weaker."

No evidence text available

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"The data showed that CYLD bound to TRAF6 constitutively, but this interaction was gradually diminished following prolonged LPA stimulation (XREF_FIG)."

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"For example, the adaptor protein p62, which is required for CYLD binding to TRAF6, regulates the DUB activity of CYLD by promoting CYLD ubiquitination [ xref ]."

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"Further, TRAF6 interacts with CYLD to mediate BCL3 deubiquitination, which facilitates the cytoplasmic accumulation of BCL3 and represses BCL3 and p50 complex mediated cyclin D1 transcription."

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"CYLD, a de-ubiquitinating enzyme, physically interacts with p62, the CYLD and TRAF6 complex negatively regulates TRAF6 ubiquitination and regulates the sustained inhibitory actions of NF-kB and NFATc1 during RANKL induced osteoclastogenesis."

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"The interaction of CYLD with TRAF6 was dependent upon p62, thus defining a mechanism that accounts for decreased activity of CYLD in the absence of p62."

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"p62 interacts with CYLD and promotes the binding of CYLD to TRAF6, and this molecular interplay requires the C-terminal domain of p62 [ xref ]."

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"Because CYLD is not interacting with TRAF6 ( xref ), it will be interesting to explore whether TRIP interacts with TRAF6."

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"p62 interacts with CYLD and promotes the binding of CYLD to TRAF6, and this molecular interplay requires the C-terminal domain of p62 [XREF_BIBR]."

No evidence text available

No evidence text available

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"Later work studying signaling through the toll like receptor 2 (TLR2) performed cell based experiments to demonstrate that CYLD binds to TRAF6 and TRAF7 and that depletion of CYLD increases the ability of transfected TRAF6 or TRAF7 to activate an NFkappaB dependent reporter gene [XREF_BIBR]."

No evidence text available

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"Given that TRAF6 interacts with CYLD in some cells, it is possible that CYLD recruitment was mediated by the initial interaction with TRAF6."

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"On the other hand, in ovarian cancer cells and glioblastoma cells that show persistent NF-kappaB activity and high levels of TRIP6, both A20 and CYLD bind to TRAF6 very weakly."

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"Considering that TRAF6 induces angiogenesis and TRAF6 function is regulated by CYLD, we hypothesized that Sal A may also inhibit angiogenesis by promoting CYLD-TRAF6 interaction."

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"For example, CYLD directly associates and deubiquitinates NEMO and TRAF-6, thus inhibiting TNF-alpha-induced nuclear factor-kappaB (NF-kappaB) signaling [13,15-17]."

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"To address this issue, we expressed FLAG-TRAF6 in HEK293T cells and treated cells with LPA for various times to determine how TRAF6 associates with deubiquitinase A20 or CYLD."

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"The miRNA-19b targeted the deubiquitinating enzyme cylindromatosis (CYLD) in the aorta and broke the ubiquitination balance of CYLD-TRAF6."

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"Perhaps because the levels of CYLD and the binding of CYLD to TRAF6 were already reduced following LPA stimulation, we only observed a reduction of this association by TRIP6 overexpression in unstimulated cells."