IndraLab

Statements

OTUD6B leads to the deubiquitination of KIFC1. 5 / 5
| 5
reach
"Whilst modulating OTUD6B had little effect on KIFC1 stability or ubiquitination in interphase cells (Fig. EV5I,J), acute ubiquitination of KIFC1 during mitosis (Appendix Fig. S7D) was decreased by overexpression of catalytically active OTUD6B (Fig. 6C) and increased by OTUD6B depletion (Fig. 6B) particularly for K11 polyubiquitin (Fig. 6E)."
39789388
reach
"This evidence for catalytic activity of OTUD6B towards K11-linked ubiquitin in other contexts is consistent with its ability to reduce mitotic KIFC1 polyubiquitination (Fig. 6) as the APC/C appends K11-linked and branched chains to substrates (Jin et al, 2008; Meyer and Rape, 2014)."
39789388
reach
"We speculate that such a mechanism may enable cancer cells to maintain a check on KIFC1 ubiquitylation during anaphase and telophase, to ensure that supernumerary centrosomes remain clustered so that chromosomes are accurately divided into daughter cells.However, we found that OTUD6B depletion could increase KIFC1 polyubiquitination not only at mitotic exit, but also in prometaphase arrested cells (Fig. 6B) when it had the strongest effect on KIFC1 degradation."
39789388
reach
"In the converse experiment, we found that overexpression of wild-type, but not catalytic dead, OTUD6B could decrease polyubiquitination of GFP-KIFC1 during mitotic exit (Fig. 6C)."
39789388
reach
"Importantly, the polyubiquitination of GFP-KIFC1 in the presence of K11-only ubiquitin was robustly increased by OTUD6B depletion (Fig. 6E)."
39789388