TY - JOUR
T1 - Identification of eukaryotic elongation factor-2 as a novel cellular target of lithium and glycogen synthase kinase-3
AU - Karyo, Racheli
AU - Eskira, Yael
AU - Pinhasov, Albert
AU - Belmaker, R. H.
AU - Agam, Galila
AU - Eldar-Finkelman Hagit, H.
N1 - Funding Information:
This work was supported by the FP7 EU grant no. 223276 “NeuroGSK3”, and the Israeli Ministry of Health , grant no 300000-5187 . This work is in partial fulfillment of the PhD requirements for R. Karyo.
PY - 2010/12
Y1 - 2010/12
N2 - Inhibition of glycogen synthase kinase-3 (GSK-3) is thought to be a major consequence of the biological and clinical activity of the mood stabilizer lithium, however, lithium and GSK-3 may activate distinct cellular pathways. We employed a proteomic method to uncover new downstream targets of lithium, and then examined how these proteins are related to GSK-3. Proteomic analysis identified eukaryotic elongation factor-2 (eEF-2) as a cellular target of lithium. This was verified in SH-SY5Y cells and animal models. In cells, lithium decreased eEF-2 phosphorylation at its key inhibitory site, threonine 56, and blocked the enhancement of eEF-2 phosphorylation normally coupled with stress conditions such as nutrient and serum deprivation. Unexpectedly, inhibition of GSK-3 enhanced eEF-2 phosphorylation, and overexpression of GSK-3α or GSK-3β resulted in a strong reduction in eEF-2 phosphorylation. Chronic administration of lithium reduced the hippocampal fraction of phospho-eEF-2 (phospho-eEF-2/total eEF-2) twofold in two different mouse strains. In summary, unexpectedly eEF-2 is activated by both lithium and GSK-3, whereas, lithium treatment and inhibition of GSK-3 have opposing effects on eEF-2.
AB - Inhibition of glycogen synthase kinase-3 (GSK-3) is thought to be a major consequence of the biological and clinical activity of the mood stabilizer lithium, however, lithium and GSK-3 may activate distinct cellular pathways. We employed a proteomic method to uncover new downstream targets of lithium, and then examined how these proteins are related to GSK-3. Proteomic analysis identified eukaryotic elongation factor-2 (eEF-2) as a cellular target of lithium. This was verified in SH-SY5Y cells and animal models. In cells, lithium decreased eEF-2 phosphorylation at its key inhibitory site, threonine 56, and blocked the enhancement of eEF-2 phosphorylation normally coupled with stress conditions such as nutrient and serum deprivation. Unexpectedly, inhibition of GSK-3 enhanced eEF-2 phosphorylation, and overexpression of GSK-3α or GSK-3β resulted in a strong reduction in eEF-2 phosphorylation. Chronic administration of lithium reduced the hippocampal fraction of phospho-eEF-2 (phospho-eEF-2/total eEF-2) twofold in two different mouse strains. In summary, unexpectedly eEF-2 is activated by both lithium and GSK-3, whereas, lithium treatment and inhibition of GSK-3 have opposing effects on eEF-2.
KW - EEF-2
KW - GSK-3
KW - Lithium
KW - Phosphorylation
KW - Protein synthesis
UR - http://www.scopus.com/inward/record.url?scp=77957963266&partnerID=8YFLogxK
U2 - 10.1016/j.mcn.2010.08.004
DO - 10.1016/j.mcn.2010.08.004
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C2 - 20708687
AN - SCOPUS:77957963266
SN - 1044-7431
VL - 45
SP - 449
EP - 455
JO - Molecular and Cellular Neuroscience
JF - Molecular and Cellular Neuroscience
IS - 4
ER -