IndraLab

Statements


AKT1 inhibits TSC2. 10 / 14
2 | 8

"We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines."

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"Liu et al. evolved a model in which AKT1 induces the 14–3-3-mediated proteolytic degradation of TSC2."

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"Phosphorylated active AKT1 deactivates TSC2 through phosphorylation at S939 and T1462, which results in binding of TSC2 to 14-3-3 [45, 46]."

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"Akt1 dependent phosphorylation negatively regulates the functioning of TSC1 and TSC2, 2 other factors involved in insulin signaling."

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"AKT1 promotes the degradation of TSC2, resulting in decreased activation of Rho, and also regulates the stability and protein expression of the transcription factor NFAT1 (Astrinidis et al., 2002; Lar[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Insulin and growth factors result in protein kinase B (PKB or Akt) phosphorylation, which inhibits tuberin (tuberous sclerosis 2 or TSC2)."

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"AKT1 blocks mTORC1 inhibitor TSC2 (30) 172 and further supports the suggestion that up-regulation of mTORC1 components has antiviral effects.173As AKT1 inhibition results in BECN1 up-regulation and autophagy induction (10, 31), SARS-CoV-2 174 growth inhibition was expected."
| DOI

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"Akt1 has been found to inhibit cell migration via phosphorylation of the actin binding factor paladin, as well as via the regulation of the nuclear factors of activated T-cells, ERK and TSC2 [XREF_BIBR]."

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"On the other hand, AKT1 was shown to inhibit migration and metastasis by regulating integrin beta1, MMP9, tuberous sclerosis complex 2 (TSC2), and palladin [XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR]."
| PMC

"We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines."
Kinase-active AKT1 inhibits TSC2. 1 / 1
1 |

"Akt then phosphorylates tuberin on three residues (S939, S1130 and T1462 of full length human tuberin), and this inhibits the tuberin-hamartin complex through an as-yet-undefined mechanism (reviewed in [8])."