IndraLab

Statements

RHEB binds USP4. 8 / 8
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"Moreover, AKT inhibitor (MK2206) disrupted the interaction between USP4 and Rheb (Supplementary information, Fig.  xref ), and promoted Rheb ubiquitination (Supplementary information, Fig.  xref )."
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"Furthermore, interaction of USP4 and Rheb was examined by immunoprecipitation assay (Figure  xref )."
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"The interaction between USP4 and Rheb in cells was confirmed by both in vivo co-IP assay and in vitro GST pull down assay (Fig.  xref )."
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"To examine whether the phosphorylation of USP4 at Ser445 affects the interaction between USP4 and Rheb, we generated a USP4 dephospho-mimetic mutant (USP4-S445A) and a phospho-mimetic mutant (USP4-S445D)."
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"However, our data showed that only USP4 interacted with Rheb (Supplementary information, Fig. S xref )."
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"Since our data showed that Rheb ubiquitination was inhibited by EGF treatment (Fig.  xref ), we examined whether the interaction between USP4 and Rheb was affected by EGF treatment and found that EGF treatment promoted their interaction at both endogenous and exogenous level (Fig.  xref and Supplementary information, Fig.  xref )."
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"Interestingly, our data showed that USP4-S445A barely bound to Rheb (Fig.  xref )."
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"Moreover, our data suggest that the DUSP domain of USP4 accounts for the interaction between Rheb and USP4 (Supplementary information, Fig.  xref )."
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