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AKT phosphorylates USP14. 32 / 34
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rlimsp
"The Akt phosphorylation site in USP14 from different species as predicted by Scansite."
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sparser
"Since USP14 is a negative regulator of the UPS ( xref ; xref , xref ) 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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"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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"To test whether Akt could phosphorylate USP14, we overexpressed USP14 and an activated Akt (Myr-Akt) in HEK293T cells, and performed a quantitative phosphoproteomic analysis (XREF_FIG)."
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rlimsp
"(D) Inhibition of Akt decreased exogenous USP14 phosphorylation."
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rlimsp
"Phosphorylation of ubiquitin-specific protease-14 (USP14) by Akt activates USP14 DUB activity."
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sparser
"Remarkably, Akt-dependent phosphorylation of USP14 elevates the catalytic activity of proteasome-associated USP14 beyond this level."
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reach
"USP14 is a deubiquitinating enzyme which presents reversible association with proteasome, and can inhibit the proteasome activity via trimming K48 ubiquitin chains on the proteasome‐bound substrates.36, 37 Recent study revealed that USP14 could be phosphorylated and activated by AKT, and could negatively regulate autophagy in neurodegenerative diseases.32, 38 Herein, we validated that SPAG5‐AS1 regulated the de‐ubiquitination of SPAG5 relying on USP14, and therefore activated AKT/mTOR signalling."
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sparser
"Thus, to fully understand the signaling pathways and the interactomes of USP14 involved in cancer cell growth and metabolism, further research on the phosphorylation of USP14 by AKT along with inhibition and knockdown studies of USP14 may be necessary."
| PMC
sparser
"Taken together, these data show that phosphorylation of USP14 by Akt is important for this kinase to negatively regulate the UPS in a ubiquitin-dependent manner."
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reach
"Similar to the inhibition of USP14, blocking AKT, which mediates the phosphorylation of USP14, was also reported to rescue the activity of NHEJ-DDR proteins during autophagy in PTEN-deficient cells (Sharma et al., 2020)."
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sparser
"The phosphorylation of USP14 by Akt was further confirmed using an Akt phosphorylation-consensus motif (R××S/T) antibody ( xref )."
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"The phosphorylation of USP14 by Akt was further confirmed using an Akt phosphorylation-consensus motif (RxxS/T) antibody (XREF_FIG)."
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sparser
"Phosphorylation of USP14 by AKT enhances its deubiquitinase activity ( xref ; xref )."
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rlimsp
"Since USP14 is a negative regulator of the UPS (Koulich et al., 2008; Lee et al., 2010, 2011) 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."
26523394
reach
"Remarkably, Akt dependent phosphorylation of USP14 elevates the catalytic activity of proteasome associated USP14 beyond this level."
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reach
"Since Akt is dramatically activated in PTEN deficient cancer cells, the control of USP14 phosphorylation by Akt may provide a mechanism for cancer cells with PTEN loss, one of the most common cancer mutations, to control global intracellular proteostasis by regulating protein degradation through proteasomes."
26523394
reach
"Taken together, these data show that phosphorylation of USP14 by Akt is important for this kinase to negatively regulate the UPS in a ubiquitin dependent manner."
26523394
rlimsp
"Since Akt is dramatically activated in PTEN-deficient cancer cells, the control of USP14 phosphorylation by Akt may provide a mechanism for cancer cells with PTEN loss, one of the most common cancer mutations, to control global intracellular proteostasis by regulating protein degradation through proteasomes."
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rlimsp
"To test whether Akt could phosphorylate USP14, we overexpressed USP14 and an activated Akt (Myr-Akt) in HEK293T cells, and performed a quantitative phosphoproteomic analysis (Figure 1—figure supplement 1B)."
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rlimsp
"Since Akt can be activated by a wide range of growth factors and is under negative control by phosphoinosotide phosphatase PTEN, we suggest that regulation of UPS by Akt-mediated phosphorylation of USP14 may provide a common mechanism for growth factors to control global proteostasis and for promoting tumorigenesis in PTEN-negative cancer cells."
26523394
rlimsp
"Taken together, these data show that phosphorylation of USP14 by Akt is important for this kinase to negatively regulate the UPS in a ubiquitin-dependent manner."
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rlimsp
"(F) Akt phosphorylates USP14 in vitro."
26523394
sparser
"Since Akt is dramatically activated in PTEN-deficient cancer cells, the control of USP14 phosphorylation by Akt may provide a mechanism for cancer cells with PTEN loss, one of the most common cancer mutations, to control global intracellular proteostasis by regulating protein degradation through proteasomes."
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rlimsp
"(B) Akt phosphorylates USP14 at S432 in vivo."
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reach
"Thus, to fully understand the signaling pathways and the interactomes of USP14 involved in cancer cell growth and metabolism, further research on the phosphorylation of USP14 by AKT along with inhibition and knockdown studies of USP14 may be necessary."
| PMC
rlimsp
"Remarkably, Akt-dependent phosphorylation of USP14 elevates the catalytic activity of proteasome-associated USP14 beyond this level."
26523394
reach
"Phosphorylation of USP14 by AKT enhances its deubiquitinase activity (Huang et al., 2011; Xu et al., 2015)."
33169399
rlimsp
"The phosphorylation of USP14 by Akt was further confirmed using an Akt phosphorylation-consensus motif (R××S/T) antibody (Figure 2—figure supplement 1A)."
26523394
sparser
"To test whether Akt could phosphorylate USP14, we overexpressed USP14 and an activated Akt (Myr-Akt) in HEK293T cells, and performed a quantitative phosphoproteomic analysis ( xref )."
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rlimsp
"(E) In vitro kinase assay to detect Akt phosphorylation of USP14 by phospho-Ser432-specific antibody and phos-tag-containing gels."
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reach
"Phosphorylation and activation of USP14 mediated by Akt may provide a mechanism for promoting tumorigenesis in cancer cells with PTEN loss [XREF_BIBR]."
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