Sentences with phrase «mtor phosphorylation»

Phosphorylation of mTOR is increased in response to leucine [20], an excellent substrate for SLC6A14; as such, our findings that mTOR phosphorylation is markedly decreased in Slc6a14 − / − tumours indicate that the tumours suffer from amino acid deprivation.

Chiang and Abraham (43) have recently shown that mTOR phosphorylation at Ser2448 is blocked by rapamycin, and this effect is independent of AKT activation status.

AKT activation contributes to mTOR phosphorylation in ALCL cells.

C and D, inhibition of AKT1 expression or activity decreases mTOR phosphorylation.

Not exact matches

Binding of raptor to mTOR is necessary for phosphorylation of 4E - BP1 and p70S6K (Fig. 7).

The phosphorylation status of all mTOR signaling proteins was determined as negative, positive, and strongly positive (+ +) depending on the presence and staining intensity of signal (Table 1).

Because treatment with rapamycin also led to decreased AKT phosphorylation in ALK + ALCL cells in our in vitro study, it is tempting to speculate that an effector protein downstream of mTOR - raptor may contribute directly or indirectly to AKT activation.

mTOR - raptor complex is sensitive to rapamycin and regulates cell growth, in part, by phosphorylation of p70S6K and subsequently rpS6 and 4E - BP1, thus promoting protein translation.

mTOR - rictor complex (composed of mTOR, rictor, and GβL) is not rapamycin sensitive and modulates cell survival and proliferation by direct phosphorylation of AKT on Ser473 and by facilitating AKT phosphorylation on Thr308 by PDK1 in vitro (13).

Treatment of the Karpas 299 and SU - DHL1 cell lines with increasing concentrations of rapamycin, an inhibitor of the mTOR - raptor complex, resulted in a marked concentration - dependent decrease of the phosphorylation levels of mTOR, p70S6K, 4E - BP1, and total eIF4E (Fig. 4A).

The phosphorylation status of mTOR, 4E - BP1, p70S6K, and rpS6 was immunohistochemically examined in 31 ALK + ALCL tumors.

We observed that the phosphorylation level of AKT significantly correlated with the phosphorylation level of mTOR and rpS6 as well as with expression of total 4E - BP1 and eIF4E in ALK + ALCL tumors.

Infection of both cell lines with adeno - myrAkt resulted in substantially increased of Ser473p - AKT levels (A) associated with increased phosphorylation (activation) of mTOR, p70S6K, and rpS6 (B).

A and B, phosphorylation and subcellular localization of mTOR signaling proteins in ALCL cell lines.

The translation initiation factor, eIF4E, is an indirect target of mTOR because it is released by phosphorylation of its repressor 4E - BP1 by mTOR - raptor complex, thereby stimulating cap - dependent translation (7, 11, 12).

Silencing of total mTOR gene expression by siRNA decreased AKT phosphorylation.

Constitutive activation of AKT resulted in a substantial increase in the phosphorylation of mTOR, p70S6K, and rpS6 (Fig. 3A and B).

We also show that inhibition of mTOR with rapamycin, as well as silencing mTOR gene product expression using mTOR - specific small interfering RNA, decreased phosphorylation of mTOR signaling proteins and induced cell cycle arrest and apoptosis in ALK + ALCL cells.

In agreement with this observation, recently Sarbassov et al. (13) have shown that rictor - mTOR (but not mTOR - raptor) complex directly phosphorylates AKT on Ser473 and facilitates Thr308 phosphorylation by PDK1 in vitro.

C and D, the phosphorylation status of mTOR, p70S6K, 4E - BP1, and rpS6 was assessed immunohistochemically in a series of 31 ALK + ALCL tumors.

However, the PI3K - AKT - mTOR pathway model seems to be more complex, as recent evidence suggests that rictor - mTOR complex directly phosphorylates AKT on Ser473 and facilitates Thr308 phosphorylation by PDK1 in vitro and mTOR is directly phosphorylated by p70S6K at Ser2448.

The balance between kinase and phosphatase activities determines the rate of phosphorylation of the insulin receptor kinase domain and several downstream targets including the phosphatidylinositol phosphates, the serine / threonine kinase Akt1 and the mTOR.

Activation of the insulin receptor leads to sequential activation of a number of protein and lipid kinases, including the serine / threonine kinases Akt1 and Akt2, which not only stimulate mTOR and thus downregulate autophagic protein catabolism (and thus cysteine supplies), but elicit phosphorylation (inhibition) of FOXO1, a transcription factor that induces expression of proteins involved in both of the proteolysis recycling pathways: the autophagic / lysosomal pathway and the ubiquitin - proteasomal pathway.

Endocrine responses and acute mTOR pathway phosphorylation to resistance exercise with leucine and whey.

BetaTOR has been shown to increase the phosphorylation of mTOR, thus activating the mTOR signaling pathway in muscle.

The discordant mTOR - p70S6K phosphorylation with protein only and protein feedings with alcohol is not unprecedented given we [8] and others [43] have shown that mTOR - S6K phosphorylation often parallels changes in MPS but does not always reflect either the magnitude or duration of the increased MPS signal in humans.

Furthermore, phosphorylation states of intracellular regulators of muscle protein synthesis (mTOR, 70 - kDa S6 kinase, and eIF4E - BP1) were similar in pigs that consumed a leucine - supplemented, low - protein diet or a high - protein diet without additional leucine, highlighting the potential synthetic effect resulting from increased leucine intake.