IndraLab

Statements

USP14 binds TAB2. 8 / 8
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"In contrast, the interaction between USP14 and TAB 2 induces deubiquitination of TAB 2, resulting in the inhibition of activation of NF-κB and p38 (Figure xref I, right)."
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"Although USP14 and TRAF6 interaction did not affect TRAF6 ubiquitination, we found that USP14 interacted with TAB 2 and induced deubiquitination of TAB 2."
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"These results suggest that USP14 interacts with the internal domain of TAB 2 as depicted in Figure xref C. We then examined whether USP14 affected the deubiquitination of TAB 2."
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"Although USP14 and TRAF6 interaction did not affect TRAF6 ubiquitination, we found that USP14 interacted with TAB 2 and induced deubiquitination of TAB 2."
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"In contrast, the interaction between USP14 and TAB 2 induces deubiquitination of TAB 2, resulting in the inhibition of activation of NF-kappaB and p38."
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"HA-TAB 2 protein was specifically precipitated with Myc-USP14 protein, indicating that USP14 interacted with TAB 2."
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"These results demonstrate that USP14 and TAB 2 interaction can induce deubiquitination of TAB 2 that is ubiquitinated by TRAF6, leading to inhibition of NF-κB activation induced by TLR4 as depicted in Figure xref B."
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"HA-TAB 2 protein was specifically precipitated with Myc-USP14 protein (Figure xref B, lane 2), indicating that USP14 interacted with TAB 2."
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