scholarly journals Differential kinetics of changes in the state of phosphorylation of ribosomal protein S6 and in the rate of protein synthesis in MPC 11 cells during tonicity shifts.

1984 ◽  
Vol 3 (1) ◽  
pp. 95-100 ◽  
Author(s):  
J. Kruppa ◽  
M.J. Clemens
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
The State ◽  
Ribosomal Protein S6 ◽  
Kinetics Of

scholarly journals Haloperidol Regulates the State of Phosphorylation of Ribosomal Protein S6 via Activation of PKA and Phosphorylation of DARPP-32

2011 ◽  
Vol 36 (12) ◽  
pp. 2561-2570 ◽  
Author(s):  
Emmanuel Valjent ◽  
Jesus Bertran-Gonzalez ◽  
Heather Bowling ◽  
Sébastien Lopez ◽  
Emanuela Santini ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
The State ◽  
Ribosomal Protein S6

scholarly journals Death-Associated Protein Kinase Phosphorylates Mammalian Ribosomal Protein S6 and Reduces Protein Synthesis†

Biochemistry ◽  
2006 ◽  
Vol 45 (45) ◽  
pp. 13614-13621 ◽  
Author(s):  
Andrew M. Schumacher ◽  
Anastasia V. Velentza ◽  
D. Martin Watterson ◽  
John Dresios
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Ribosomal Protein ◽  
Ribosomal Protein S6 ◽  
Death Associated Protein Kinase

scholarly journals Stimulation of skeletal muscle myofibrillar protein synthesis, p70 S6 kinase phosphorylation, and ribosomal protein S6 phosphorylation by inhibition of myostatin in mature mice

2009 ◽  
Vol 296 (3) ◽  
pp. E567-E572 ◽  
Author(s):  
Stephen Welle ◽  
Kerri Burgess ◽  
Sangeeta Mehta
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Myofibrillar Protein ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
S6 Kinase ◽  
P70 S6 Kinase ◽  
Ribosomal Protein S6 ◽  
The Mean ◽  
Myofibrillar Protein Synthesis

Knocking out myostatin activity during development increases the rate of muscle protein synthesis. The present study was done to determine whether postdevelopmental loss of myostatin activity stimulates myofibrillar protein synthesis and the phosphorylation of some of the proteins involved in regulation of protein synthesis rate. Myostatin activity was inhibited for 4 days, in 4- to 5-mo-old male mice, with injections of an anti-myostatin antibody (JA16). The mean myofibrillar synthesis rate increased 19% ( P < 0.01) relative to the mean rate in saline-treated mice, as determined by incorporation of deuterium-labeled phenylalanine. JA16 increased phosphorylation of p70 S6 kinase (S6K) and ribosomal protein S6 (rpS6) 1.9-fold ( P < 0.05). It did not affect phosphorylation of eukaryotic initiation factor 4E-binding protein-1 or Akt. Microarrays and real-time PCR analyses indicated that JA16 administration did not selectively enrich levels of mRNAs encoding myofibrillar proteins, ribosomal proteins, or translation initiation and elongation factors. Rapamycin treatment did not affect the rate of myofibrillar protein synthesis whether or not the mice received JA16 injections, although it eliminated the phosphorylation of S6K and rpS6. We conclude that the normal level of myostatin activity in mature muscle is sufficient to inhibit myofibrillar synthesis rate and phosphorylation of S6K and rpS6. Reversal of the inhibition of myofibrillar synthesis with an anti-myostatin antibody is not dependent on mTOR activation.

scholarly journals Molecular mechanisms relating to amino acid regulation of protein synthesis

2019 ◽  
Vol 32 (2) ◽  
pp. 183-191 ◽  
Author(s):  
Yangchun Cao ◽  
Shimin Liu ◽  
Kai Liu ◽  
Imtiaz Hussain Raja Abbasi ◽  
Chuanjiang Cai ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Translation Initiation ◽  
Molecular Mechanisms ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Signalling Pathways ◽  
Control Of Gene Expression ◽  
Ribosomal Protein S6 ◽  
New Findings

AbstractSome amino acids (AA) act through several signalling pathways and mechanisms to mediate the control of gene expression at the translation level, and the regulation occurs, specifically, on the initiation and the signalling pathways for translation. The translation of mRNA to protein synthesis proceeds through the steps of initiation and elongation, and AA act as important feed-forward activators that are involved in many pathways, such as the sensing and the transportation of AA by cells, in these steps in many tissues of mammals. For the translation, phosphorylation of eukaryotic translation initiation factor 2α (eIF2α) is a critical molecule that controls the translation initiation and its functions can be regulated by some AA. Another control point in the mRNA binding step in the translation initiation is at the regulation by mammalian target of rapamycin, which requires a change of phosphorylation status of ribosomal protein S6. In fact, the change of phosphorylation status of ribosomal protein S6 might be involved in global protein synthesis. The present review summarises recent work on the molecular mechanisms of the regulation of protein synthesis by AA and highlights new findings.

Sign in / Sign up

Export Citation Format

Share Document