IndraLab

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USP10 binds SMAD4. 18 / 18
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"Further evidence revealed that USP10 directly binds to Smad4 and stabilizes Smad4 through deubiquitination [46]."
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"Therefore, these results collectively revealed the specific interaction between USP10 and Smad4 both at the endogenous and exogenous levels."
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"As USP10 directly binds to Smad4 and regulates its protein stability, we hypothesized that USP10 exerts such regulation through the deubiquitination of Smad4."
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"Further evidence revealed that USP10 directly binds to Smad4 and stabilizes Smad4 through deubiquitination [46] ."
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"As USP10 directly binds to Smad4 and regulates its protein stability, we hypothesized that USP10 exerts such regulation through the deubiquitination of Smad4."
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"USP10 interacts with Smad4 in vivo ."
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"USP10 directly interacts with SMAD4 and stabilizes it to promote HCC proliferation and metastasis (149) ."
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"Further analysis showed that USP10 directly interacts with Smad4 and stabilizes it through the cleavage of its proteolytic ubiquitination, thus promoting HCC metastasis."
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"More importantly, the interaction between the endogenous USP10 and endogenous Smad4 was further demonstrated in our Co‐IP analyses (Fig. 3D)."
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"In addition, we also observed an interaction between the Flag‐tagged Smad4 and endogenous USP10 (Fig. xref C)."
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"As shown in Fig. 3A, USP10 could be indeed coprecipitated from cell lysates together with HA‐tagged Smad4 by anti‐HA antibody, suggesting an exogenous interaction between USP10 and Smad4."
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"More importantly, the interaction between the endogenous USP10 and endogenous Smad4 was further demonstrated in our Co‐IP analyses (Fig. xref D)."
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"USP10 directly interacts with Smad4 and reverses the polymerization of the ubiquitin chain linked to proteolytic Lys48, resulting in its stabilization and the activation of TGF-β signaling, which promotes HCC metastasis [46] ."
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"Mechanistically, USP10 directly binds to Smad4 and reverts the proteolytic Lys‐48‐linked polyubiquitin chain on Smad4, thus leading to its stabilization."
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"As shown in Fig. xref B, USP10‐C424A also efficiently interacted with Smad4 similar as USP10‐WT, suggesting the catalytic activity of USP10 is not required for Smad4 binding."
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"Further analysis showed that USP10 directly interacts with Smad4 and stabilizes it through the cleavage of its proteolytic ubiquitination, thus promoting HCC metastasis."
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"Therefore, these results collectively revealed the specific interaction between USP10 and Smad4 both at the endogenous and exogenous levels.3.4 USP10 deubiquitinates and stabilizes Smad4 through the removal of Lys-48-linked ubiquitin chains."
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sparser
"As shown in Fig. xref A, USP10 could be indeed coprecipitated from cell lysates together with HA‐tagged Smad4 by anti‐HA antibody, suggesting an exogenous interaction between USP10 and Smad4."
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