IndraLab

Statements

USP13 is ubiquitinated. 10 / 10
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"NEDD4 undergoes K29-linked auto-ubiquitination at K1279 and serves as a scaffold for recruiting USP13 to form a NEDD4-USP13 deubiquitination complex, which subsequently cleaves the K48-linked poly-ubiquitin chains from PIK3C3 at K419, thus stabilizing PIK3C3 to promote autophagy. the ubiquitination of USP13; however, NEDD4 appears to be its own substrate for ubiquitination, and the catalytic activity of NEDD4 is required for its auto-ubiquitination."
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"On the other hand, coexpression of USP10 with USP13 has a much less pronounced effect on ubiquitination of USP13 (data not shown)."
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"Protein interaction experiments demonstrated that USP13 could co-immunoprecipitate with endogenous TopBP1, and in vitro deubiquitination enzyme experiments showed that WT-USP13 could deubiquitinate TopBP1, while CA-USP13 could not, highlighting the requirement for USP13 ubiquitination activity ( xref )."
35445009
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"USP13 and gp78 control ubiquitination of Ubl4A."
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"We noticed that NEDD4-1 did not affect the ubiquitination of USP13, suggesting that USP13 is not a direct substrate of NEDD4-1 ( Figure S5 A)."
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"LPS-induced USP13 degradation was attenuated by actinomycin D ( xref ), suggesting a new protein induced by LPS regulates USP13 ubiquitination."
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"To investigate the molecular regulation of the unknown protein, which regulates USP13 ubiquitination and degradation, we examined several factors related to transcriptional regulation."
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"We found that short time exposure of LPS did not trigger USP13 degradation, suggesting that an immediate LPS signaling through TLR4 does not contribute to USP13 ubiquitination and degradation."
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"From the time points of LPS’ effect, we hypothesized that activation of JNK by LPS does not directly affect USP13 ubiquitination."
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"To investigate whether LPS regulates USP13 degradation through ubiquitination, we examined the effect of LPS on USP13 ubiquitination."
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