IndraLab

Statements



sparser
"One possibility is that phosphorylation enhances USP37 binding to its ubiquitinated substrates by altering the configuration of its three ubiquitin-interacting motifs (UIMs) spanning Ser 704 -Ser 723 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Detecting endogenous ubiquitin-protein conjugates that coimmunoprecipitate with transfected wild-type and UIM mutant USP37 proteins suggested only UIM2 and UIM3, rather than UIM1, permit the interaction between USP37 and ubiquitin-protein conjugates in a synergistic manner."
| PMC

sparser
"To determine whether the physical association between USP37 and WAPL is dependent on the ubiquitin-binding activity of USP37, the same mutations were introduced into full-length FLAG-USP37 and express[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"The deubiquitinase activity of USP37 and its ubiquitin interacting motifs are essential for the deubiquitination of SAMHD1, whereas the phosphorylation state of USP37 does not influence its activity."

sparser
"Because USP37 stabilizes chromatin-associated WAPL and the ubiquitin-binding activities of USP37 are important for its association with WAPL, we next aimed to determine whether USP37 regulates deubiqu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"In the case of K48-linked substrates, binding of the UIMs to the proximal Ub increased catalytic efficiency of USP37 largely through k cat and to a lesser degree through K M . This result was somewhat counter-intuitive since we expected that binding of the UIMs of USP37 to Ub to have a more pronounced effect on K M (a proxy for binding affinity) since others have shown that UIM mutations perturbed the ability to pull down Ub conjugates xref ."

sparser
"Mutations in UIM2 and/or UIM3 perturb USP37 binding to endogenous ubiquitin–protein conjugates [ xref , xref , xref ]."

sparser
"The issue of how the binding of the UIMs of USP37 to the proximal Ub of K48 di-Ub enhances activity remains an open question."

sparser
"We expected that, if USP37 deubiquitylates WAPL, the ubiquitin-binding activities of USP37 would be critical for the interaction between USP37 and WAPL."