IndraLab

Statements


ZRANB1 binds HECTD1.
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"Although we attempted to validate the interaction between endogenous TRABID and endogenous HECTD1, none of the four TRABID antibodies that we tried could detect endogenous TRABID (Data not shown)."
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"First, we validated the interaction between TRABID and HECTD1 using GST-tagged TRABID NZF 1–3, in line with our previous work (Fig. 6C)."

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"Thus, this study identifies HECTD1 as a mammalian E3 ligase that assembles branched K29/K48 chains and also establishes TRABID-HECTD1 as a DUB/E3 pair regulating K29 linkages."
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"Therefore, we further explored the TRABID-HECTD1 interaction in order to reconcile and also expand on these observations."
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"Although we attempted to validate the interaction between endogenous TRABID and endogenous HECTD1, none of the four TRABID antibodies that we tried could detect endogenous TRABID (Data not shown)."
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No evidence text available
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"Additionally, it was shown that the Trabid, Hectd1, and APC complex interacts with proteins composing the striatin interacting phosphatase and kinase (STRIPAK) complex that regulates cortical actin cytoskeleton dynamics [XREF_BIBR]."
ZRANB1 ubiquitinates HECTD1.
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ZRANB1 ubiquitinates HECTD1. 1 / 1
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"Having established that TRABID NZF 1 to 3 is required for binding HECTD1 in cells and that catalytic dead TRABID traps polyubiquitinated HECTD1, we then validated this data in the context of HECTD1 's newly identified ubiquitin ligase activity using a pull-down approach (XREF_FIG, C and D; Fig.S3)."
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ZRANB1 increases the amount of HECTD1.
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ZRANB1 increases the amount of HECTD1. 1 / 1
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"Importantly, this decrease in HECTD1 protein levels could be rescued by re-expression of pEGFP-TRABID WT but not pEGFP-Empty vector alone, indicating that TRABID directly regulates HECTD1 levels (XREF_FIG D)."
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ZRANB1 deubiquitinates HECTD1.
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ZRANB1 deubiquitinates HECTD1. 1 / 1
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"The E3 ubiquitin ligase <span class="match term1">HECTD1</span> was then validated as a substrate of <span class="match term0">TRABID</span> and used UbiCREST and Ub-AQUA proteomics to show that <span class="match term1">HECTD1</span> preferentially assembles K29- and K48-linked ubiquitin chains"