IndraLab

Statements


4 | 1 6

sparser
"Eleven confirmed hits inhibited the USP8::CHMP1B interaction within a range of 30% to 70% inhibition at 50 µM, while they were inactive on a set of other PPI interfaces demonstrating the feasibility of specifically disrupting this particular interface."

No evidence text available

sparser
"As anticipated from earlier studies, a deletion of the MIM (Microtubule Interacting and Trafficking domain Interacting Motif) domain or mutation of two conserved leucine residues, L192 and L195, in this domain respectively abolished or strongly impeded the USP8::CHMP1B interaction."

sparser
"The USP8 MIT domain binds tightly to CHMP1B and more weakly to a subset of other CHMPs ( xref )."

sparser
"Interaction of CHMP1B with USP8 occurs via α-helices 4, 5, and 6 of CHMP1B."

No evidence text available

No evidence text available

No evidence text available

reach
"Full-length CHMP1B and alpha-helices 4, 5 and 6 interacted with Flag-USP8 in this assay (XREF_FIG)."

sparser
"The function of USP8 at the endocytic pathway level partly relies on binding to and deubiquitination of the Endosomal Sorting Complex Required for Transport (ESCRT) protein CHMP1B. In the aim of finding chemical inhibitors of the USP8::CHMP1B interaction, we performed a high-throughput screening campaign using an HTRF® assay to monitor the interaction directly in lysates of cells co-expressing both partners."

sparser
"Identification of chemicals breaking the USP8 interaction with its endocytic substrate CHMP1B."