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Statements

AKT binds CYLD. 20 / 25
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"In this study we provided experimental evidences for direct interaction between Akt and CYLD, and also showed that CYLD does directly deubiquitinate Akt under both endogenous and exogenous conditions."
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"We next determined whether Akt associates with CYLD."
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"As shown in xref , endogenous CYLD indeed directly interacts with endogenous Akt and S. pneumoniae treatment increased their direct interaction."
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"Moreover, we found that endogenous Akt interacted with CYLD under serum starved conditions in a reciprocal immunoprecipitation assay (XREF_FIG)."
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"The finding that CYLD interacts with Akt and suppresses ubiquitination of Akt prompted us to determine whether CYLD prevents phosphorylation of Akt in response to growth factor stimulation."
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"CYLD interacts with and keeps Akt in a hypoubiquitinated and inactive stage by directly removing Akt ubiquitination under serum starvation conditions."
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"As shown in XREF_FIG, endogenous CYLD indeed directly interacts with endogenous Akt and S. pneumoniae treatment increased their direct interaction."
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"We next determined whether endogenous CYLD directly interacts with endogenous Akt and if such a direct interaction is further increased on S. pneumoniae treatment by performing Duolink in vivo protein protein interaction detection assay XREF_BIBR XREF_BIBR and co-immunoprecipitation assay."
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"These results suggest that CYLD interacts with Akt under serum starvation conditions and dissociates from Akt upon growth factor stimulation, which may allow E3 ligases to bind to and ubiquitinate Akt."
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"Because IGF-1 disrupts the interaction between Akt and CYLD, we also determined whether phosphorylation of Akt attenuated (or disrupted) its interaction with CYLD."
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"Results in xref showed that CYLD and Akt are indeed physically associated with each other in epithelial cells co-transfected with HA-CYLD and Flag-Akt."
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"The interaction between CYLD and Akt was lost after 15 minutes of IGF-1 treatment (XREF_FIG), whereas the interaction between Akt and TRAF6 was induced at the same time point (6), suggesting that CYLD and TRAF6 may compete with each other for Akt binding."
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"However, the interaction between Akt and CYLD is independent of the ubiquitination and phosphorylation status of Akt."
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"We found that CYLD interacts with Akt under serum-free condition, but dissociates from Akt upon growth factor stimulation."
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"Both wild-type and the constitutively active Akt mutant T308D and S473D (Akt-DD) interacted with CYLD (XREF_SUPPLEMENTARY), suggesting that the phosphorylation of Akt does not affect Akt and CYLD interaction."
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"In this study we provided experimental evidences for direct interaction between Akt and CYLD, and also showed that CYLD does directly deubiquitinate Akt under both endogenous and exogenous conditions."
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"We next determined whether endogenous CYLD directly interacts with endogenous Akt and if such a direct interaction is further increased on S. pneumoniae treatment by performing Duolink in vivo protein–protein interaction detection assay xref xref and co-immunoprecipitation assay."
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"To further determine how CYLD negatively regulates Akt, we first examined whether CYLD physically interacts with Akt by performing co-immunoprecipitation experiments."
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"Indeed, we found that TRAF6 overexpression inhibited the binding of CYLD to Akt in a dose dependent manner (XREF_FIG)."
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"CYLD bound to both non ubiquitinated and ubiquitinated Akt forms (XREF_FIG), and both wild-type Akt and the ubiquitination deficient K8R mutant (6) interacted with CYLD (XREF_FIG)."
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