IndraLab

Statements

USP4 binds SART3. 31 / 35
11 | 11 9
sparser
"However, when ALAL-1 was depleted, the SART3-mediated nuclear translocation of USP4 was partially impaired ( xref ), while the interaction between SART3 and USP4 was not affected by depletion of ALAL-1 ( xref ), indicating that ALAL-1 is involved in USP4 relocalization without impairing SART3-USP4 interaction in bulk."
32858747
biogrid
No evidence text available
27060135
sparser
"The USP4 sart3 complex helps to recruit the substrate PRP3, as well as increase the deubiquitinating activity of USP4 ( xref ; xref )."
33681193
biogrid
No evidence text available
27990632
reach
"In order to identify the exact NLS required for the nuclear import of SART3 as well as the SART3 and USP4 complex, we have co-purified NLS of SART3 with ImpA (residues 70-498 of mouse importin-alpha) and the complex was crystallized."
27060135
sparser
"USP4 binds SART3 at the opposite surface of the HAT-C dimer interface utilizing the β-structured linker between the DUSP and the UBL domains."
27060135
biogrid
No evidence text available
20595234
reach
"These findings suggest SART3 binds to both USP15 and USP4, and this may lead to deubiquitination of PRP31 and PRP3 simultaneously."
28088760
sparser
"The interaction analysis showed that USP4 and SART3 form a complex with the majority of the U4/U6-snRNP components such as PRP31, PRP3 and PRP4 ( xref )."
28088760
sparser
"To have a better understanding of the interaction between ALAL-1 and SART3 and USP4, we performed coimmuno-FISH experiments coupled with confocal microscopy."
32858747
biogrid
No evidence text available
28088760
reach
"USP4 binds SART3 at the opposite surface of the HAT-C dimer interface utilizing the beta structured linker between the DUSP and the UBL domains."
27060135
sparser
"A similarly unified DUSP-UBL interaction surface was also suggested for the USP4 interaction with the U4/U6 recycling protein SART3 ( xref )."
23105109
reach
"Moreover, as a substrate recruiting factor of USP15 either, SART3 can simultaneously bind USP4 and USP15, serving as a platform to deubiquitinate PRP31 and PRP3."
33681193
sparser
"In this process, USP15 makes a complex with USP4 and SART3 that serves as a platform for the efficient splicing of chromosome segregation-related genes, such as Bub1 and α-tubulin, by stabilizing the U4/U6."
33946990
sparser
"Interestingly, the pathways found to be affected by either ALAL-1 or SART3 depletion were previously reported in different studies to be modulated by SART3 directly or indirectly through its interacting partner USP4 ( xref ; xref ; xref ; xref ), suggesting that the interaction of ALAL-1 with SART3 could be regulating the SART3–USP4 complex."
32858747
reach
"We next examined whether SART3 forms a complex with USP15 and USP4 simultaneously using sequential immunoprecipitation."
28088760
biogrid
No evidence text available
19615732
reach
"Moreover, it was reported that Sart3, Usp4 and Usp15 form a complex in order to de-ubiquitinate Prp3 and Prp31 simultaneously."
| PMC
biogrid
No evidence text available
20595234
biogrid
No evidence text available
28088760
biogrid
No evidence text available
27060135
reach
"The interaction analysis showed that USP4 and SART3 form a complex with the majority of the U4/U6-snRNP components such as PRP31, PRP3 and PRP4."
28088760
reach
"USP15 and USP4 form a complex with SART3."
28088760
sparser
"SART3 is known to function as a recruiting as well as a targeting factor for USP4 in pre-mRNA processing, and USP4 does not appear to contain an NLS of its own, it is plausible that USP4 interaction with SART3 allows for USP4 nuclear translocation."
27060135
biogrid
No evidence text available
20595234
biogrid
No evidence text available
23022198
reach
"In order to verify the importance of the beta-hairpin linker between the DUSP and UBL domains as seen in the crystal structure of SART3 and USP4 complex, we generated a series of mutants, e.g. the linkers of USP4 (124 HGLFVKHC 131) and USP15 (124 QGMFVKHC 131) replaced by the USP11 linker (186 LPNIQ 190) and vice versa, denoted as USP4 L11 and USP15 L11, USP11 L4 and USP11 L15."
27060135
reach
"SART3 is known to function as a recruiting as well as a targeting factor for USP4 in pre-mRNA processing, and USP4 does not appear to contain an NLS of its own, it is plausible that USP4 interaction with SART3 allows for USP4 nuclear translocation."
27060135
biogrid
No evidence text available
20595234
reach
"The crystal structure of USP4 and SART3 complex in this study reveals that the linker between the DUSP and UBL domains of USP4 forms a beta-structure, and the residues forming the beta-hairpin loop, namely L126, F127, V128 and H130, are the binding determinant for SART3 binding."
27060135