IndraLab

Statements

USP4 binds USP15. 24 / 35
7 | 10 14
sparser
"USP15 and USP4 form a complex with SART3."
28088760
sparser
"However, Tip110 was found to interact with and promote nuclear translocation of USP4 and USP15 but not USP11, and this is due to β-hairpin of the linker region of the DUSP and UBL domains of both USP4 and USP15 proteins that were associated with the HAT domain of Tip110 ( xref , xref , xref , xref ) In addition, the binding of USP15 to Tip110 is 20-fold stronger than USP4 ( xref )."
35530338
sparser
"We further investigated the possibility of USP15 interacting with other parts of USP4 using a GST-pull down assay."
28088760
sparser
"However, when full length USP4 synthesized with IVT/T was used, there was no binding ( xref ) suggesting that the interaction between USP15 and USP4 is indirect."
28088760
sparser
"To examine the effect of endogenous SART3, the interaction between USP4 and USP15 was examined by immunoprecipitation after depletion of SART3 using siRNA."
28088760
sparser
"The depletion of SART3 hampered the interaction between USP15 and USP4 (Figure xref and  xref )."
28088760
sparser
"For example, SART3 has been shown to form a complex with USP4 and USP15 by binding their DUSPs through its C-terminal region."
34666042
reach
"We found that USP15 interacts with both overexpressed and endogenous USP4."
28088760
reach
"To examine whether USP15 interact with USP4 directly, we first carried out an ITC experiment using the DUSP-UBL domains of the two proteins."
28088760
reach
"Moreover, it was reported that Sart3, Usp4 and Usp15 form a complex in order to de-ubiquitinate Prp3 and Prp31 simultaneously."
| PMC
reach
"Furthermore, they demonstrate that AKT phosphorylation of USP4 enhances the binding of USP4 to USP15 and that overexpression of USP15 increases USP4 stability."
28923280
reach
"However, when full length USP4 synthesized with IVT/T was used, there was no binding (XREF_SUPPLEMENTARY) suggesting that the interaction between USP15 and USP4 is indirect."
28088760
reach
"To examine the effect of endogenous SART3, the interaction between USP4 and USP15 was examined by immunoprecipitation after depletion of SART3 using siRNA."
28088760
reach
"The depletion of SART3 hampered the interaction between USP15 and USP4."
28088760
sparser
"These findings suggest SART3 binds to both USP15 and USP4, and this may lead to deubiquitination of PRP31 and PRP3 simultaneously."
28088760
reach
"SART3 has been stated mostly as a U4/U6 recycling factor, but our data show that SART3 serves as a substrate targeting factor as well as acts as a platform for USP15 and USP4 binding."
28088760
sparser
"SART3 has been stated mostly as a U4/U6 recycling factor ( xref ), but our data show that SART3 serves as a substrate targeting factor as well as acts as a platform for USP15 and USP4 binding."
28088760
sparser
"We discovered USP11-specific peptides harboring consensus motifs that do not interact with either paralog USP4 or USP15, and we identified a novel binding site in the USP11 N-terminal ubiquitin-like domain."
30373771
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"USP4 can form stable homodimers and can also interact with USP11 and USP15."
27155333
sparser
"Furthermore, they demonstrate that AKT phosphorylation of USP4 enhances the binding of USP4 to USP15 and that overexpression of USP15 increases USP4 stability."
28923280
sparser
"Therefore, exploring factors that bind to the C-terminal regions of USP4 and USP15 may provide insights into elucidating their functions within cells."
38310689
reach
"Importantly, USP4 could bind to itself and also interact with USP11 and USP15, and thus may be part of a DUB complex when exerting its function."
24756567
sparser
"A USP15–USP4 amino acid sequence alignment in the SL region reveals the only difference to be a cysteine residue (USP15 Cys 352 ), which replaces a serine (Ser 394 ) in USP4 ( xref D and)."
30228188
sparser
"Interestingly, USP4 and USP15, the paralogs of USP11 [ xref ], are also associated with osteogenesis [ xref , xref ]; however, there have been no prior reports on USP11 and its functions related to bone remodeling to our knowledge."
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