
IndraLab
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"However, although DAAM1-actin binding is not required for its inhibitory activity on USP10, our experiments demonstrate that DAAM1 may sequester USP10 to actin-stress fibers: Treatment with TGFβ1 enhanced the proximity between USP10 and DAAM1 and promoted co-localization with actin-stress fibers (Fig. 4 and Supplemental Fig 4) and DAAM1 knockdown caused a concomitant loss of USP10 from stress fibers (Fig. 5)."
reach
"We speculate that kinase-mediated phosphorylation regulates the activity of USP10, allowing USP10 to regulate mitotic proteins independent of its expression.E3–DUB interactions allow fine-tuning of the ubiquitylation status of a common substrate, which generally involves a non-competitive binding mechanism (antagonistic pattern) [11, 22, 23, 40]."