IndraLab

Statements

TNFAIP3 binds TRAF6 and CYLD. 7 / 7
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"Nonetheless, depletion of TRIP6 can significantly enhance the association of A20 or CYLD with TRAF6 in ovarian cancer cells and promote the binding of A20 to TRAF6 in glioblastoma cells, suggesting that targeting TRIP6 may prove to be an effective strategy to restore the function of A20 and CYLD in restricting the NF-κB activity in these cancer cells."
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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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"Nonetheless, depletion of TRIP6 by either shRNA ( xref ) or Cas9/sgRNA ( xref ) not only enhanced the association of TRAF6 with A20, but also with CYLD in untreated and treated cells, suggesting a significant role for TRIP6 in antagonizing the binding of TRAF6 to both A20 and CYLD in ovarian cancer cells."
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"On the other hand, in ovarian cancer cells and glioblastoma cells that show persistent NF-κB activity and high levels of TRIP6, both A20 and CYLD bind to TRAF6 very weakly."
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"In this regard, here we provide evidence that the adaptor protein TRIP6 (thyroid hormone receptor-interacting protein 6), a specific interacting protein of the LPA2 receptor but not other LPA receptors, recruits TRAF6 to the LPA2 receptor and enhances the E3 ligase activity of TRAF6 by antagonizing the association of A20 and CYLD to TRAF6."
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"Overexpression of TRIP6 interferes with the recruitment of A20 to TRAF6, whereas depletion of TRIP6 enhances the association of TRAF6 with A20 and CYLD, and eliminates LPA-promoted K63-linked polyubiquitination of TRAF6."
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"In contrast, depletion of TRIP6 by TRIP6-specific shRNA or Cas9/sgRNA greatly enhances the association of TRAF6 with A20 and CYLD, and attenuates lysophosphatidic acid-induced muclear factor-κB and JNK/p38 activation in ovarian cancer cells."
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