Results 31 to 40 of about 15,232 (136)

GCN2 is activated by methyl jasmonate through GCN1 and reactive oxygen species in Arabidopsis thaliana

Scientific Reports
Plant growth and productivity rely on rapid energy management strategies to adapt dynamic environments. Previous work in Arabidopsis thaliana identified a fast-regulatory switch linking cytosolic translation and reactive oxygen species (ROS) signaling ...
Daniel Rincon Diaz, Morgan E. Wynn, Emmanuel Asiedu, Teressa K. Akuoko, Ansul Lokdarshi   +4 more
doaj   +1 more source

Interactions of the heme-regulated eIF-2 alpha kinase with heat shock proteins in rabbit reticulocyte lysates.

Journal of Biological Chemistry, 1992
Inhibition of protein synthesis in rabbit reticulocyte lysates occurs in response to a variety of conditions including heme deficiency, addition of oxidants, and heat stress. The inhibition of translation is due to the activation of a heme-regulated protein kinase (HRI) which specifically phosphorylates the alpha-subunit of the eukaryotic initiation ...
R L, Matts, Z, Xu, J K, Pal, J J, Chen
openaire   +2 more sources

Mechanism of action of an eukaryotic initiation factor-2 (eIF-2) associated 67 kDa glycoprotein (p67) and an eIF-2 kinase (dsI).

Indian journal of biochemistry & biophysics, 1995
Mechanism of regulation of eIF-2 alpha-subunit phosphorylation by dsI and p67 was studied. The results are as follows: (1) At low dsI concentration, p67 protected equimolar concentration of eIF-2. (2) At high dsI concentration, dsI efficiently phosphorylated eIF-2 alpha-subunit even when equimolar concentrations of both p67 and eIF-2 were present ...
A, Chakraborty, D, Saha, A, Bose, R E, Hileman, M, Chatterjee, N K, Gupta   +5 more
openaire   +1 more source

The stress sensor GCN2 differentially controls ribosome biogenesis in colon cancer according to the nutritional context

Molecular Oncology
Nutrient availability is a key determinant of tumor cell behavior. While nutrient‐rich conditions favor proliferation and tumor growth, scarcity, and particularly glutamine starvation, promotes cell dedifferentiation and chemoresistance.
Marie Piecyk, Mouna Triki, Pierre‐Alexandre Laval, Cedric Duret, Joelle Fauvre, Laura Cussonneau, Christelle Machon, Jerôme Guitton, Nicolas Rama, Benjamin Gibert, Gabriel Ichim, Frederic Catez, Fleur Bourdelais, Sebastien Durand, Jean‐Jacques Diaz, Isabelle Coste, Toufic Renno, Serge N. Manié, Nicolas Aznar, Stephane Ansieau, Carole Ferraro‐Peyret, Cedric Chaveroux   +21 more
doaj   +1 more source

Disulfide bond formation in the regulation of eIF-2 alpha kinase by heme.

The Journal of biological chemistry, 1989
The inhibition of the autophosphorylation of the heme-regulated eukaryotic initiation factor (eIF)-2 alpha kinase (HRI) by hemin is very similar to that produced by thiol oxidation by diamide. The results obtained from the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis of unphosphorylated and phosphorylated HRI under reducing and
J J, Chen, J M, Yang, R, Petryshyn, N, Kosower, I M, London   +4 more
openaire   +1 more source

Hsp90 mediates activation of the heme regulated eIF-2 alpha kinase during oxidative stress.

Indian journal of biochemistry & biophysics, 2010
The heme-regulated inhibitor (HRI), a member of the eIF-2 alpha kinase family is crucial for regulating protein synthesis during stress. In addition to heme, stress proteins Hsp90 and Hsp70 are known to regulate HRI. The present study aims to determine the physical association of these Hsps in the regulation of HRI activation during oxidative stress ...
A P, Kulkarni, S P, Mittal, T P A, Devasagayam, J K, Pal   +3 more
openaire   +1 more source

Effects of glucose 6-phosphate and hemin on activation of heme-regulated eIF-2 alpha kinase in gel-filtered reticulocyte lysates.

Journal of Biological Chemistry, 1984
In heme-deficient reticulocyte lysates, protein synthesis initiation is inhibited due to the activation of a heme-regulated protein kinase which blocks protein synthesis by the specific phosphorylation of the alpha-sub-unit of eukaryotic initiation factor 2 (eIF-2 alpha).
A M, Michelson, V, Ernst, D H, Levin, I M, London   +3 more
openaire   +2 more sources

Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2 alpha (eIF-2 alpha) kinase. Evidence for multitissue expression.

Journal of Biological Chemistry, 1994
Reticulocytes contain an eukaryotic initiation factor-2 alpha (eIF-2 alpha) kinase that is negatively regulated by hemin. This protein kinase, which has been termed heme-regulated inhibitor and heme-controlled repressor (HCR), has a strong inhibitory effect on the initiation of protein synthesis and plays an important role in translational control in ...
Mellor, H, Flowers, K M, Kimball, S R, Jefferson, L S   +3 more
openaire   +2 more sources

Regulation of protein synthesis in rabbit reticulocyte lysates [PDF]

FEBS Letters, 1986
The heme‐regulated protein kinase, which specifically phosphorylates the 38‐kDa subunit of initiation factor eiF‐2, can utilize adenosine 5′‐O‐(3‐thiotriphosphate) (ATP[γS]) as a substrate. The rate of thiophosphorylation is 5‐6‐times slower than that observed with ATP.
openaire   +2 more sources

Kinetics of Phosphorylation of eIF-2 by the hemin-controlled repressor and casein kinase II. Inhibition by hemin and 2,3-diphosphoglyceric acid.

Journal of Biological Chemistry, 1982
The kinetics of phosphorylation of eukaryotic initiation factor 2 (eIF-2) by two cyclic nucleotide-independent protein kinases from rabbit reticulocytes have been studied. The hemin-controlled repressor (HCR) and casein kinase II phosphorylate the alpha and beta subunits of eIF-2, respectively.
, Gonzatti-Haces MIrn, J A, Traugh
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