| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-164 |
Sentence |
denotes |
Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. |
| T2 |
165-307 |
Sentence |
denotes |
Protein synthesis consumes a high proportion of the metabolic energy of mammalian cells, and most of this is used by peptide chain elongation. |
| T3 |
308-422 |
Sentence |
denotes |
An important regulator of energy supply and demand in eukaryotic cells is the AMP-activated protein kinase (AMPK). |
| T4 |
423-668 |
Sentence |
denotes |
The rate of peptide chain elongation can be modulated through the phosphorylation of eukaryotic elongation factor (eEF) 2, which inhibits its activity and is catalyzed by a specific calcium/calmodulin-dependent protein kinase termed eEF2 kinase. |
| T5 |
669-828 |
Sentence |
denotes |
Here we show that AMPK directly phosphorylates eEF2 kinase, and we identify the major site of phosphorylation as Ser-398 in a regulatory domain of eEF2 kinase. |
| T6 |
829-915 |
Sentence |
denotes |
AMPK also phosphorylates two other sites (Ser-78 and Ser-366) in eEF2 kinase in vitro. |
| T7 |
916-1136 |
Sentence |
denotes |
We develop appropriate phosphospecific antisera and show that phosphorylation of Ser-398 in eEF2 kinase is enhanced in intact cells under a range of conditions that activate AMPK and increase the phosphorylation of eEF2. |
| T8 |
1137-1212 |
Sentence |
denotes |
Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. |
| T9 |
1213-1379 |
Sentence |
denotes |
Although cardiomyocytes appear to contain a distinct isoform of eEF2 kinase, it also contains a site corresponding to Ser-398 that is phosphorylated by AMPK in vitro. |
| T10 |
1380-1491 |
Sentence |
denotes |
Stimuli that activate AMPK and increase eEF2 phosphorylation within cells increase the activity of eEF2 kinase. |
| T11 |
1492-1651 |
Sentence |
denotes |
Thus, AMPK and eEF2 kinase may provide a key link between cellular energy status and the inhibition of protein synthesis, a major consumer of metabolic energy. |
