IndraLab

Statements


4 | 1 5

sparser
"OTUD1 binds to YAP and removes its K63-ubiquitin chain in a Hippo-independent manner, indicating that OTUD1 is a negative regulator of YAP signaling."

reach
"OTUD1 binds to YAP and removes its K63-ubiquitin chain in a Hippo-independent manner, indicating that OTUD1 is a negative regulator of YAP signaling."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

sparser
"OTUD1 binds YAP and reverses its K63 ubiquitination."

sparser
"This non-proteolytic ubiquitination can be reversed by the binding and interaction between deubiquitinase OTUD1 and YAP1; OTUD1 decreases YAP1 stability, and attenuates the cell proliferation and tumor-growth activity of YAP1 ( xref )."

sparser
"We further validated the interaction between OTUD1 and YAP in vivo and in vitro."

sparser
"Moreover, His-YAP protein purified from bacteria could be pulled down by GST-OTUD1, but not by GST, in an in vitro binding assay (Fig.  xref ), suggesting that OTUD1 directly interacts with YAP."