This study does not mention anything about PTOR and the body loves being in hemostasis. Also any excess protein will eventually undergo gluconeogenesis. If all this protein contributes to muscle hypertrophy, then there would be a massive number of people all over the place. This study is vague and forgets about many other important factors regarding anabolism and hypertrophy. That's why AAS is so good in building muscle because it prevents catabolism and yields to positive nitrogen balance. I can see more protein with AAS and Insulin would yield to more protein synthesis, but without AAS and Insulin you can consume 200 grams 300 grams post work out and get nowhere.
Studies like these are misleading because they exclude the many other factors and hormones responsible for positive nitrogen balance and muscle hypertrophy. GH will yield to new muscle cells, AAS will grow these new cells, insulin will shuttle Glucose and amino acids into the muscle cell. Without the hormones we use, a person can eat 1000 grams of protein a day and not see much improvement.
You mention "PTOR" - do you mean mTOR?
If you read the actual study, you'll see (Figure 5) they measured just about everything possible wrt. signaling, including mTOR1 and gene expression (mRNA) related to muscle growth:
Figure 5. Dissociation between feeding-induced muscle anabolic signaling and protein translation
(A–J) Skeletal muscle phosphorylation status (ratio of phosphorylated to total protein) of mTOR (Ser2448) (A); p70S6K (Thr389) (B); p70S6K (Thr421/Ser424) (C); rpS6
(Ser235/Ser236) (D); 4E-BP1 (Thr37/Thr46) (E); and ACC (Ser79) (H) and protein content of Beclin (F), LC3b (G), Atg 12, (I), and myostatin (J) were all measured by the
western blot technique.
(K–X) Skeletal muscle relative mRNA expression (relative to 18S housekeeping gene) of mTOR (K), p70S6K (L), FOXO1 (M), MurF1 (N), MAFBx (O), PGC1-alpha
(P), myostatin (Q), Beclin1 (R), cATG12 (S), LC3b (T), LAT1SLC (U), SNAT2 (V), CD98 (W), and PAT1 (X) were all measured by real-time qPCR quantification.
And they explain:
"In contrast, we did not observe any impact of protein feeding on muscle protein signaling or muscle gene expression (Figure 5). This is in line with previous work that suggests that the molecular response in skeletal muscle to protein ingestion is short lived (<4 h).16,37 Here, we extend these data by demonstrating that the muscle anabolic response to protein ingestion is sustained well beyond (R12 h) the frequently reported transient changes in molecular signaling. Collectively, these data suggest substantial divergence in the time course of the molecular response and the actual metabolic response to feeding (Figure 5Y). Therefore, the magnitude and/or time course of muscle molecular responses should not be used as a proxy to evaluate the magnitude of the postprandial anabolic response to feeding."
But, as I noted in my post above, they didn't muscle MUSCLE Protein breakdown, but measured at the whole body level:
"The postprandial increase in plasma amino acid availability has a negligible impact on whole-body protein breakdown or postprandial amino acid oxidation rates. "
-S