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AKT activates USP14. 17 / 18
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"Accordingly, when Usp14 is activated by AKT, the degradation of multiple proteins appears to be suppressed [74]."
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"However, the physiological relevance of AKT-dependent activation of USP14 in the nucleus has not been examined."
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"How does this relate to the observation that USP14 is activated by AKT?"
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"As reported, USP14 was activated by AKT,32 so the non‐effect of mTOR activator on SPAG5 indicated that it was AKT, rather than mTOR that activated USP14 and led to upregulation of SPAG5 level in HG‐treated HPCs."
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"Since USP14 is a negative regulator of the UPS and we found USP14 can be phosphorylated and activated by Akt, we reasoned that Akt mediated activation of USP14 might lead to inhibition of the UPS and generally enhance the stability of many proteins."
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"Accordingly, when Usp14 is activated by AKT, the degradation of multiple proteins appears to be suppressed [ xref ]."
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"As reported, USP14 was activated by AKT, xref so the non‐effect of mTOR activator on SPAG5 indicated that it was AKT, rather than mTOR that activated USP14 and led to upregulation of SPAG5 level in HG‐treated HPCs."
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"Akt activation of USP14 has marked effects on protein turnover in cells, highlighting the physiological significance of the activity state of USP14."
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"The activation of Usp14 by AKT may provide a mechanism whereby growth signals can suppress catabolism through targeting proteasome activity."
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"Thus, Akt not only activates USP14 by a different mechanism than the proteasome, but it can cooperate with the proteasome to achieve more aggressive removal of ubiquitin from proteasome-docked substrates."
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"To validate Akt mediated activation of USP14 in cells, we coexpressed USP14 and Myr-Akt in HEK293T cells."
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"Accordingly, when Usp14 is activated by AKT, the degradation of multiple proteins appears to be suppressed [74] ."
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"The notion that USP14 may serve as a focal point for regulating proteasome activity was consistent with a recent report that the kinase Akt activates USP14 via phosphorylation 35."
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"Therefore, it remains unclear whether Ser432 phosphorylation generates a proteasome independent active form of Usp14.The activation of Usp14 by AKT may provide a mechanism whereby growth signals can s[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The notion that USP14 may serve as a focal point for regulating proteasome activity was consistent with a recent report that the kinase Akt activates USP14 via phosphorylation xref ."
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"In summary, growth signals such as insulin activate AKT, which among its many activities will potentiate USP14, likely leading to reduced protein breakdown by the proteasome."
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"Akt activation of USP14 has marked effects on protein turnover in cells, highlighting the physiological significance of the activity state of USP14."
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