IndraLab

Statements


11 1 | 63 46

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"Therefore, although Caprin1 and USP10 both bind G3BP, they have antagonistic effects on SGs."

sparser
"Thus, studies were conducted to determine if Cif inhibits USP10 activity by stabilizing the interaction between USP10 and G3BP1, and by reducing the interaction between USP10 and CFTR."

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"Studies using USP10 mutants, including USP10/77 -792 and USP10/95-792, indicate that USP10 's interaction with G3BP1 is essential for inhibition of ROS dependent apoptosis and for USP10 incorporation into stress granules."

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"Resveratrol promotes the p53-mediated apoptosis of cancer cells by acting on the USP10-binding protein G3BP1 [36]."

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"To provide additional support for the immunoprecipitation studies demonstrating that Cif increases the interaction between G3BP1 and USP10 in the early endosomal compartment, we performed bimolecular fluorescence complementation (BiFC) studies."

sparser
"Cif stabilizes USP10 and G3BP1 interaction to inhibit USP10 activity."

sparser
"Interestingly, recent work has shown that the compound resveratrol can inhibit the interaction of G3BP with USP10 by binding to the NTF2-like domain of G3BP, thereby stimulating USP10 DUB activity and stabilization of p53 [ xref ]."

sparser
"TAT-RasGAP 317–326 did not modulate binding of G3BP1 to USP10, stress granule formation or c-myc mRNA levels."

sparser
"Thus, USP10 interaction with G3BP1 and the incorporation of USP10 into stress granules are dispensable for USP10 inhibition of cytokine deprivation-induced apoptosis in FL HSPCs."

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"USP10 and Caprin1 antagonistically bind G3BP to regulate SG formation."

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"Treatment of co-transfected (YN-USP10 and YC-G3BP1) airway epithelial cells with Cif containing OMV resulted in an increase in BiFC signal, confirming an increased (4.35 +/-0.30 fold) interaction between USP10 and G3BP1 in the presence of Cif (XREF_FIG) compared to cells treated with control (Cif mutant OMV)."

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"USP10, which also binds to G3BP but inhibits stress granule assembly was identified as a suppressor."

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"Cif stabilizes USP10 and G3BP1 interaction to inhibit USP10 activity."

No evidence text available

sparser
"However, for the first time we show an in vitro interaction of the purified NTF2-like domain of G3BP1 (residues 1–139) and the N-terminal region of USP10 (residues 1–150)."

sparser
"Taken together, these data confirm our hypothesis that Cif, by enhancing G3BP1 interaction with USP10, inhibits the ability of USP10 to interact with, and deubiquitinate CFTR."

sparser
"Thus, these observations reveal that Cif stabilizes an interaction between USP10 and G3BP1, and also reduces the interaction between USP10 and CFTR."

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"As expected, the interaction between G3BP1 and USP10 decreased in HCT116 cells treated with resveratrol (XREF_FIG)."

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"Moreover, they also provide a molecular basis for the regulation of USP10 activity by assembly of the inhibitory USP10 and G3BP complex."

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"The FGDF motif of the mammalian ubiquitin-specific protease (USP10) binds to G3BP, thereby affecting the interaction of G3BP1/2 and Caprin1 to inhibit the formation of SGs (36)."

No evidence text available

sparser
"We next found that USP10 is a potent regulator of G3BP1 expression in OC cells, and confirmed that G3BP1 bound well to USP10 at endogenous level in OC cells."

sparser
"G3BP1 binds to USP10 and therefore disrupts the interaction of USP10 with p53, leading to suppression of p53 deubiquitination."

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"These results strongly indicate that resveratrol enhances USP10 mediated deubiquitination of p53 by disrupting the G3BP1 and USP10 interaction."

sparser
"G3BP1 binds to USP10 and inhibits the deubiquitination activity of USP10 ( xref )."

sparser
"TAT-RasGAP 317–326 does not affect the binding of G3BP1 to USP10."

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"Under normal conditions, G3BP1 binds to and inhibits USP10, but in stress, when both proteins become incorporated into SGs, their interaction changes and this unleashes the activity of USP10 XREF_BIBR."

No evidence text available

sparser
"Moreover, by co-transfecting cells with organelle markers, it is possible to identify the compartment where USP10 and G3BP1 interact."

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"Cif does not alter the protein abundance of USP10, but does enhance the interaction between G3BP1 and USP10 to inhibit USP10 DUB activity."

sparser
"These studies support the conclusion that Cif stabilizes the interaction between USP10 and G3BP1 in the early endosomes."

sparser
"Moreover, Cif increased the interaction between G3BP1 and USP10 by 210±12% ( xref )."

sparser
"The results suggested that G3BP1 bound well to USP10 at endogenous level ( xref )."

sparser
"Through searching for protein–protein interaction (PPI) network and Gene Expression Profiling Interactive Analysis (GEPIA) website, we found that USP10 interacted with G3BP1, and that there was a positive correlation between G3BP1 mRNA expression and USP10 mRNA expression in OC."

No evidence text available

sparser
"Mechanistically, G3BP1 forms a complex with USP10 in the progression of OC."

sparser
"Studies using USP10 mutants, including USP10/77–792 and USP10/95–792, indicate that USP10's interaction with G3BP1 is essential for inhibition of ROS-dependent apoptosis and for USP10 incorporation into stress granules ( xref )."

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"The binding of G3BP to USP10 appears to inhibit its deubiquitinating activity."

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"As a mechanism of resveratrol induced p53 expression, we revealed that resveratrol directly binds to G3BP1 and disrupts the G3BP1 and USP10 interaction, releasing USP10 which in turn results in enhanced USP10 mediated deubiquitination of p53."

sparser
"Among these, the IDP hub protein G3BP1 can form complexes with cytoplasmic phosphoprotein Caprin1 and ubiquitin peptidase USP10; the resulting control of USP10 activity contributes to a pathogenic virulence system that targets endocytic recycling of the ion channel CFTR."

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"By binding to both G3BP and PABP (a translational enhancer), USP10 could simultaneously retain mRNPs in a soluble state and prime them for translational activation and consequent removal from SGs."

sparser
"The binding of G3BP to USP10 appears to inhibit its deubiquitinating activity."

sparser
"To test if the overexpression and binding of full-length USP10 to G3BP affects the SG response, BHK cells were transfected with EGFP alone, EGFP-USP10 wt or EGFP-USP10-F10A. Transfected cells were mock stressed or stressed with sodium arsenite for 1 h before fixation and staining for G3BP-1 and TIA-1 to detect SGs."

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"USP10 binds G3BP via a conserved FGDF motif."

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"We conjectured that G3BP1 disrupts the interaction of USP10 with p53 by binding to USP10, and consequently suppresses USP10 mediated deubiquitination of p53."

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"Resveratrol, on the other hand, directly binds to G3BP1 and prevents the G3BP1 and USP10 interaction, resulting in enhanced USP10 mediated deubiquitination of p53 and consequently increased p53 expression."

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"Resveratrol enhances USP10 mediated deubiquitination of p53 by disrupting the G3BP1 and USP10 interaction."

sparser
"The DUB USP10 binds G3BP, localizes to SGs and regulates SG formation, even though the exact role of its DUB activity in this process remains controversial ( xref ; xref ; xref )."

sparser
"USP10 binds to the G3BP protein to form the USP10-G3BP1 complex, which is required for the deubiquitination of RPS2, RPS3, and RPS10."

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"Resveratrol (RSVL) directly binds to G3BP1 and prevents the interaction of G3BP1/USP10, which enhances the USP10-mediated de-ubiquitination of p53, thereby increasing p53 expression (135)."

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"TAT-RasGAP 317-326 does not affect the binding of G3BP1 to USP10."

sparser
"G3BP interacts with the deubiquitinating protease USP10 and plays an important role in the assembly of SGs."

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"Overall, our study demonstrates that resveratrol directly targets G3BP1, which in turn prevents the G3BP1 and USP10 interaction and consequently increases USP10 regulated deubiquitination of p53 (XREF_FIG)."

sparser
"Interestingly, our previous map of human protein complexes ( xref ) suggests that the known complex of G3BP, CAPRIN, and USP10 ( xref ) also physically interacts with NUFIP2, leading us to suggest the name CapGUN (i.e., CAPRIN1, G3BP2, USP10, NUFIP2)."

sparser
"Physical interaction between USP10 and G3BP, a RasGAP interacting protein overexpressed in tumors, was shown by a two-hybrid screen to suggest a link between the ubiquitination pathway and Ras-mediated signaling xref "

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"The DUB USP10 binds G3BP, localizes to SGs and regulates SG formation, even though the exact role of its DUB activity in this process remains controversial."

No evidence text available

sparser
"To determine whether this USP10 region binds G3BP, we fused the N-terminal 40 residues of human USP10 to EGFP (EGFP-USP10 1–40 )."

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"TAT-RasGAP 317-326 did not modulate binding of G3BP1 to USP10, stress granule formation or c-myc mRNA levels."

sparser
"G3BP1 interacts with USP10 in OC cells."

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"These studies support the conclusion that Cif stabilizes the interaction between USP10 and G3BP1 in the early endosomes."

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"G3BP1 binds to USP10 and inhibits the deubiquitination activity of USP10."

sparser
"In addition, several viruses (Semliki Forest, Chikungunya, and herpes simplex) encode SG-inhibiting proteins that share the same binding motif (FGDF motif) within USP10 that binds to G3BP ( xref )."

No evidence text available

sparser
"To provide additional support for the immunoprecipitation studies demonstrating that Cif increases the interaction between G3BP1 and USP10 in the early endosomal compartment, we performed bimolecular fluorescence complementation (BiFC) studies."

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"Thus, studies were conducted to determine if Cif inhibits USP10 activity by stabilizing the interaction between USP10 and G3BP1, and by reducing the interaction between USP10 and CFTR."

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"In addition, several viruses (Semliki Forest, Chikungunya, and herpes simplex) encode SG inhibiting proteins that share the same binding motif (FGDF motif) within USP10 that binds to G3BP."

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"An in vitro competition assay also showed that resveratrol inhibited the G3BP1 and USP10 interaction in a dose dependent manner (XREF_FIG)."

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"Physical interaction between USP10 and G3BP, a RasGAP interacting protein overexpressed in tumors, was shown by a two-hybrid screen to suggest a link between the ubiquitination pathway and Ras mediated signaling 61 More than half of the identified phosphoproteins were mapped to relate with cancer function."

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"Kedersha and colleagues 37 concluded that G3BP binds 40S ribosomes through its RGG region and is essential for stress granule condensation, but distinct from polysome disassembly, and the condensation process is regulated by competitive Caprin1 and USP10 binding to G3BP."
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"Thus, these observations reveal that Cif stabilizes an interaction between USP10 and G3BP1, and also reduces the interaction between USP10 and CFTR."

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"We found that USP10, the human ortholog of Ubp3p, associates with the Bre5 ortholog G3BP1, as previously reported (XREF_SUPPLEMENTARY), and also associates with the G3BP1 paralog G3BP2 (XREF_FIG)."

sparser
"Interestingly, neither Caprin1 nor USP10 binding to G3BP is needed for its association with the 40S subunit ( xref )."

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"In the article, the authors suggested that G3BP-S149 phosphorylation alters the outcome of stress granule formation by preferentially promoting the binding of G3BP to USP10 relative to Caprin1, but the authors now know that the S149E construct instead failed to rescue stress granule formation because of the unexpected S99P mutation (as shown in the Letter [Panas et al., 2019."

No evidence text available

No evidence text available

sparser
"First, published studies have shown that USP10 and G3BP1 interact in yeast and mammalian systems xref , xref , xref ."

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"Resveratrol binds to G3BP1 and interrupts the G3BP1/USP10 interaction, releasing USP10 and promoting its deubiquitinating activity, increasing p53-mediated apoptosis in melanoma (Oi et al., 2015)."

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"Three observations suggest that Cif may inhibit USP10 activity by stabilizing the interaction between USP10 and G3BP1, which inhibits USP10 DUB activity, and also reduces the interaction between USP10 and CFTR."

sparser
"Caprin1 binding to G3BP promotes SG formation, whereas USP10 binding to G3BP inhibits SG assembly."

sparser
"In contrast, binding of USP10 to G3BP promotes the soluble confirmation of G3BP, and thereby induces SG disassembly ( xref )."

sparser
"Kedersha et al. found that the proteins compete with each other for G3BP binding and that, whereas Caprin1 promotes SG formation, USP10’s interaction with G3BP inhibits SG assembly."

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"We wondered whether this interaction displaces USP10, a cellular binding partner of G3BP that also binds to the NTF2 like domain [XREF_BIBR, XREF_BIBR]."

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"It appears therefore that the FGDF mediated G3BP and USP10 complex is mutually inhibitory, with G3BP inhibiting the DUB activity of USP10 and USP10 inhibiting the SG nucleating function of G3BP."

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"Thus, USP10 interaction with G3BP1 and the incorporation of USP10 into stress granules are dispensable for USP10 inhibition of cytokine deprivation induced apoptosis in FL HSPCs."

sparser
"TAT-RasGAP₃₁₇₋₃₂₆ did not modulate binding of G3BP1 to USP10, stress granule formation or c-myc mRNA levels."

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"The USP10 and G3BP complex appears to co-immunoprecipitate with ubiquitinated species that could be substrates of USP10."

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"Kedersha et al. found that the proteins compete with each other for G3BP binding and that, whereas Caprin1 promotes SG formation, USP10 's interaction with G3BP inhibits SG assembly."

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"Interestingly, protein interactions can also prevent SG core growth, as reported by the interaction between USP10/G3BP in mammals (Kedersha et al., 2016)."

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"We therefore hypothesized that resveratrol interferes with the G3BP1 and USP10 interaction."

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"Subsequent work demonstrated that in addition to homo- and hetero-dimerization, G3BP1 and 2 interact with USP10 and Caprin1 [XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR]."

sparser
"Second, in U2OS bladder cancer cells, the interaction between G3BP1 and USP10 inactivates the deubiquitinating enzyme activity of USP10 xref ."

sparser
"A previous study reported that G3BP1 interacts directly with the N-terminus of USP10, a common protein-protein interaction domain in the USP family of DUBs for regulation of DUB activity xref ."

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"G3BP1 binds to USP10 and therefore disrupts the interaction of USP10 with p53, leading to suppression of p53 deubiquitination."

sparser
"Two proteins—Caprin1 and USP10—bind to a region of G3BP neighboring this critical phosphorylation site."

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"In addition, we show that binding of the cellular G3BP binding partner USP10 is also mediated by an FGDF motif."

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"Caprin1 and USP10 binding to G3BP is mutually exclusive : Caprin binding promotes, but USP10 binding inhibits, SG formation."

No evidence text available

sparser
"Three observations suggest that Cif may inhibit USP10 activity by stabilizing the interaction between USP10 and G3BP1, which inhibits USP10 DUB activity, and also reduces the interaction between USP10 and CFTR."

sparser
"To assess whether G3BP1 interacts with USP10 in OC or not, we used an IP assay to verify this interaction."

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"Resveratrol, on the other hand, directly binds to G3BP1 and disrupts the G3BP1 and USP10 interaction, resulting in enhanced USP10 regulated deubiquitination of p53."

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"Second, in U2OS bladder cancer cells, the interaction between G3BP1 and USP10 inactivates the deubiquitinating enzyme activity of USP10 XREF_BIBR."

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"Our results indicated that N expression abrogates G3BP1 interaction with the SG proteins CAPRIN1 and USP10 ( Figure 2C ), reinforcing the idea that N inhibits the formation of SGs in host cells by sequestering G3BPs away from their interacting SG-nucleating proteins.Since N protein contains RNA-binding domains (Kang et al., 2020) , we examined whether N interacts directly with host mRNAs."

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"Proteomic studies indicate both G3BP1 and 2 bind the 3 ' UTR of DENV genomic RNA, as well as G3BP1 interacting proteins USP10 and Caprin1 73."

No evidence text available

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"Finally, if Cif stabilizes an inhibitory interaction between G3BP1 and USP10, silencing G3BP1 should reduce the Cif induced decrease in USP10 activity as well as the Cif induced increase in ubiquitinated CFTR, and its degradation in lysosomes."

sparser
"USP10, which also binds to G3BP but inhibits stress granule assembly ( xref ) was identified as a suppressor."

No evidence text available

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"To determine whether this USP10 region binds G3BP, we fused the N-terminal 40 residues of human USP10 to EGFP (EGFP-USP10 1-40)."

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"The G3BP1/USP10 complex immunoprecipated from human U2OS cells was more resistant to acidic buffer washes than G3BP1/Caprin-1."

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"Since the binding of nsP3 and USP10 to G3BP inhibits SGs, we hypothesized that ICP8 binding might do the same."

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"Moreover, Cif increased the interaction between G3BP1 and USP10 by 210 +/-12% (XREF_FIG)."

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"USP10 's interaction with G3BP1 involves an FGDF motif within USP10 that binds a pocket within the N-terminal NTF2 like domain of G3BP1, and this binding inhibits SG condensation in response to some stresses [XREF_BIBR, XREF_BIBR]."

sparser
"USP10 binds G3BP via a conserved FGDF motif."

sparser
"In summary, these results imply that G3BP1 interacts with USP10 in OC cells."

sparser
"Caprin1 binding to G3BP promotes the formation of SGs, whereas the binding of USP10 to G3BP abolishes SG assembly."

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"The conclusions that G3BP binds 40S ribosomes through its RGG region and is essential for stress granule condensation, stress granule condensation is distinct from polysome disassembly, and the condensation process is regulated by competitive Caprin1/USP10 binding to G3BP still stand firmly."

No evidence text available

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"To provide additional support for our immunoprecipitation studies that the interaction between USP10 and G3BP1 occurs in early endosomes (XREF_FIG), BiFC experiments were performed in cells transduced with a baculovirus system expressing eRFP labeled Rab5a (an early endosomal protein) to label early endosomes."

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"Caprin1 binding to G3BP promotes SG formation, whereas USP10 binding to G3BP inhibits SG assembly."

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"However, it is important to note that the interactions between G3BP1 and USP10 or Caprin1 do not fully dictate SG disassembly or assembly, as two different laboratories recently demonstrated that the unstressed G3BP1 interactome significantly overlaps the interactome of G3BP1 during stress [XREF_BIBR, XREF_BIBR]."