IndraLab

Statements

USP25 deubiquitinates RIPK1. 11 / 11
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"USP21 suppresses TNFα-induced NF-κB activation by deubiquitinating RIP1 [ 5 ]."
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"For example, TNFAIP3, CYLD, USP3, USP4, USP15, USP25, and OTUD5 deubiquitinate key components of the IFN production pathway, including RIG-I, TRAF2, TRAF3, TRAF6, RIP1, and TRIF (reviewed in [93,94])."
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"Ubv.21.4 CDelta2 coimmunoprecipitated with USP21 in cotrans fected human embryonic kidney (HEK) 293T cells (XREF_FIG), blocked the deubiquitination of RIP1 by USP21 (XREF_FIG), and restored NF-kappaB activation (XREF_FIG)."
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"Moreover, overexpression of Ubv.21.4CΔ2, the truncated Ubv.21.4 form lacking the last two glycines, also efficiently inhibited cellular USP21 activity, blocking the deubiquitylation of RIP1 and STING by USP21 (Ernst et al., 2013; Chen et al., 2017a)."
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"Next, we showed that overexpression of AF6 abrogated RIPK1 ubiquitination in MEFs upon TNF stimulation, and further knockdown of USP21 levels rescued the reduction in RIPK1 ubiquitination caused by AF6 overexpression (Fig. 4c)."
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"Another DUB, USP21, is constitutively associated with RIP1 and de-ubiquitinates RIP1 [115] ."
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"Knockdown of USP21 enhances TNF-induced RIP1 polyubiquitination and NF-κB dependent gene expression."
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"Ubv.21.4 blocked the deubiquitination of RIP1 by USP21 and restored NF‐κB activation, showing that it acts as an inhibitor of USP21 in cells."
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"USP21 interacts with RIP1 and deubiquitinates RIP1 in a DUB dependent manner."
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"USP21 is constitutively associated with RIP1 and deubiquitinates RIP1 in vitro and in vivo."
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"A previous study showed that USP21 deubiquitylates receptor interacting protein 1, a suppressor of TNF induced NF-KB activation."
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