Melatonin synchronizes protein synthesis rhythm in hepatocyte cultures as an agonist of intercellular calcium and protein kinases

2009 ◽  
Vol 40 (3) ◽  
pp. 183-187 ◽  
Author(s):  
V. Ya. Brodsky ◽  
V. A. Golichenkov ◽  
N. D. Zvezdina ◽  
V. I. Fateeva ◽  
L. A. Mal’chenko
Keyword(s):  
Protein Synthesis ◽  
Protein Kinases ◽  
Hepatocyte Cultures ◽  
Protein Synthesis Rhythm

scholarly journals The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase

2001 ◽  
Vol 355 (3) ◽  
pp. 609-615 ◽  
Author(s):  
Yvonne L. WOODS ◽  
Philip COHEN ◽  
Walter BECKER ◽  
Ross JAKES ◽  
Michel GOEDERT ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Kinases ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Initiation Factor ◽  
Glycogen Synthase Kinase 3 ◽  
General Role ◽  
Protein Tau ◽  
Microtubule Associated Protein Tau ◽  
Protein Synthesis Initiation

The substrate specificity of glycogen synthase kinase 3 (GSK3) is unusual in that efficient phosphorylation only occurs if another phosphoserine or phosphothreonine residue is already present four residues C-terminal to the site of GSK3 phosphorylation. One such substrate is the ε-subunit of rat eukaryotic protein-synthesis initiation factor 2B (eIF2Bε), which is inhibited by the GSK3-catalysed phosphorylation of Ser535. There is evidence that GSK3 is only able to phosphorylate eIF2Bε at Ser535 if Ser539 is already phosphorylated by another protein kinase. However, no protein kinases capable of phosphorylating Ser539 have so far been identified. Here we show that Ser539 of eIF2Bε, which is followed by proline, is phosphorylated specifically by two isoforms of dual-specificity tyrosine phosphorylated and regulated kinase (DYRK2 and DYRK1A), but only weakly or not at all by other ‘proline-directed’ protein kinases tested. We also establish that phosphorylation of Ser539 permits GSK3 to phosphorylate Ser535in vitro and that eIF2Bε is highly phosphorylated at Ser539in vivo. The DYRK isoforms also phosphorylate human microtubule-associated protein tau at Thr212in vitro, a residue that is phosphorylated in foetal tau and hyperphosphorylated in filamentous tau from Alzheimer's-disease brain. Phosphorylation of Thr212 primes tau for phosphorylation by GSK3 at Ser208in vitro, suggesting a more general role for DYRK isoforms in priming phosphorylation of GSK3 substrates.

scholarly journals Inhibition of protein synthesis and activation of stress-activated protein kinases by onnamide A and theopederin B, antitumor marine natural products

2005 ◽  
Vol 96 (6) ◽  
pp. 357-364 ◽  
Author(s):  
Kun-Hyung Lee ◽  
Shinichi Nishimura ◽  
Shigeki Matsunaga ◽  
Nobuhiro Fusetani ◽  
Sueharu Horinouchi ◽  
...  
Keyword(s):  
Natural Products ◽  
Protein Synthesis ◽  
Protein Kinases ◽  
Marine Natural Products ◽  
Inhibition Of Protein Synthesis

The Administration of Semax and HLDF-6 Peptides to Rats Regulates Protein Synthesis Rhythm in Hepatocytes and Corrects Senescent Disturbances

2020 ◽  
Vol 51 (2) ◽  
pp. 99-105
Author(s):  
V. Y. Brodsky ◽  
Y. A. Zolotarev ◽  
L. A. Malchenko ◽  
L. A. Andreeva ◽  
D. S. Lazarev ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Synthesis Rhythm

Plasma Protein Synthesis in Isolated Hepatocyte Cultures

1974 ◽  
Vol 46 (4) ◽  
pp. 23P-23P
Author(s):  
K. N. Jeejeebhoy ◽  
J. Ho ◽  
G. R. Greenberg ◽  
M. J. Phillips ◽  
A. Bruce-Robertson ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Plasma Protein ◽  
Hepatocyte Cultures

Protein synthesis rhythm

1975 ◽  
Vol 55 (1) ◽  
pp. 167-200 ◽  
Author(s):  
W.Ya. Brodsky
Keyword(s):  
Protein Synthesis ◽  
Protein Synthesis Rhythm
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