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Phosphorylation of S202/203 of AKT1S1 by PKM2 released AKT1S1 from raptor (show RPTOR Proteins) and facilitated its binding to 14-3-3 (show YWHAQ Proteins), resulted in hormonal- and nutrient-signals independent activation of mTORC1 signaling and led accelerated oncogenic growth and autophagy inhibition in cancer cells.
The frameshift mutation detected in the current study would result in a premature stop of amino-acid synthesis in AKT1S1 protein and hence resembles a typical loss-of-function mutation.
Supporting this idea, we identified a downstream target of the TGFb (show TGFB1 Proteins)-miR (show MLXIP Proteins)-96 signaling pathway to be AKT1S1 mRNA, whose translated protein is a negative regulator of mTOR (show FRAP1 Proteins) kinase.
This review discusses the role of PRAS40 and possible feedback mechanisms, and alterations in AKT (show AKT1 Proteins)/PRAS40/mTOR (show FRAP1 Proteins) signaling that have been implicated in the pathogenesis of tumor progression. [review]
Findings indicate that dual phosphorylation of PRAS40 by Akt (show AKT1 Proteins) and mTORC1 promotes formation of a nuclear-specific PRAS40- and RPL11 (show RPL11 Proteins)-containing complex distinct from mTORC1 that inhibits the RPL11 (show RPL11 Proteins)-HDM2-p53 (show TP53 Proteins) pathway.
PRAS40 as a regulator of insulin (show INS Proteins) sensitivity in hSkMC
PRAS40 contains a functional nuclear export signal. Furthermore, enforced nuclear accumulation of PRAS40 impairs insulin (show INS Proteins) action, thereby substantiating the function of this protein in the regulation of insulin (show INS Proteins) sensitivity.
Data suggest that PRAS40 modulates insulin (show INS Proteins) action in skeletal muscle; knockdown of PRAS40 inhibits insulin (show INS Proteins) action in cultured myotubes and is associated with up-regulation of IRS1 (insulin receptor substrate 1 (show IRS1 Proteins)) degradation via proteasome proteolysis.
WISP1 (show WISP1 Proteins) governs PRAS40 by sequestering PRAS40 intracellularly through post-translational phosphorylation.
study found tuberin and PRAS40 to be potent anti-apoptotic gatekeepers in early stem-cell differentiation; data allow new insights into the regulation of early stem-cell maintenance and differentiation and identify a new role of the tumor suppressor tuberin and the oncogenic protein PRAS40
PRAS40 appears to reduce brain injury following ischemic stroke by converting cell signaling from Akt (show AKT1 Proteins) to mTOR (show FRAP1 Proteins)
PRAS40 treatment improves hepatic insulin (show INS Proteins) sensitivity and reduces systemic hyperglycaemia in obese mice.
PRAS40 phosphorylation acts as a molecular switch allowing mTORC1 activation during physiological growth, opening up unique possibilities for therapeutic regulation of the mTORC1 complex to mitigate pathologic myocardial hypertrophy by PRAS40
Naturally secreted amyloid-beta increases mammalian target of rapamycin (mTOR (show FRAP1 Proteins)) activity via a PRAS40-mediated mechanism.
These results suggest that a reduction in PRAS40 specifically impairs myoblast protein synthesis, cell cycle, proliferation and differentiation to myotubes.
PRAS phosphorylation and its interaction with pAkt and 14-3-3 might play an important role in neuroprotection mediated by NGF in apoptotic neuronal cell death after transient focal cerebral ischemia
overexpression of SOD1 (show SOD1 Proteins) may affect the PRAS pathway after transient focal cerebral ischemia by reducing the direct oxidative reaction to pPRAS after reperfusion injury
PRAS40 is an important regulator of insulin (show INS Proteins) sensitivity of the Akt (show AKT1 Proteins)-mTOR (show FRAP1 Proteins) pathway and a potential target for the treatment of cancers, insulin (show INS Proteins) resistance and hamartoma syndromes.
PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding.
after mTORC1 kinase activation by upstream regulators, PRAS40 is phosphorylated directly by mTOR (show FRAP1 Proteins), thus contributing to the relief of PRAS40-mediated substrate competition.
AKT1S1 is a proline-rich substrate of AKT (MIM 164730) that binds 14-3-3 protein (see YWHAH, MIM 113508) when phosphorylated (Kovacina et al., 2003
AKT1 substrate 1 (proline-rich)
, proline-rich AKT1 substrate 1
, 40 kDa proline-rich AKT substrate
, proline-rich AKT substrate
, PKB/Akt substrate 40