IndraLab

Statements

OTUD6B deubiquitinates LIN28B. 5 / 5
| 5
reach
"Although OTUD6B regulates pVHL independently of its DUB activity (Liu et al, 2020), the catalytic cysteine of OTUD6B is required to limit ubiquitination of β-TrCP (Li et al, 2023) and LIN28B (Paulmann et al, 2022), as we found for KIFC1 (Fig. 6C)."
39789388
reach
"Specificity of this deubiquitylation event was ascertained by overexpression of the catalytic inactive OTUD6B mutant (C158A), which deubiquitylated LIN28B to a substantially smaller extent (Fig 2C)."
36059274
reach
"OTUD6B readily deubiquitylated LIN28B in this in vitro reconstituted system, suggesting that LIN28B is a direct substrate (Fig 2E)."
36059274
reach
"Together, these data suggest that LIN28B is a cell cycle regulated protein with highest abundance at the G1/S transition and early S‐phase and that OTUD6B specifically deubiquitylates LIN28B at the G1/S transition of the cell cycle to procure its stability."
36059274
reach
"Together, these data suggest that MCTS1 can enhance the stability of LIN28B during the G1/S transition by interacting with OTUD6B.Using a ubiquitin-K48 specific antibody, we observed lentivirus-mediat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
37634410