PhosphoPlus ® GCN2 (Thr899) Antibody Duet #26168
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Background
Phosphorylation of the eukaryotic initiation factor 2 (eIF2) alpha subunit is a well-documented mechanism of downregulating protein synthesis under a variety of stress conditions. Kinases activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), and hemin deficiency (HRI) can phosphorylate the eIF2 alpha subunit (1,2). GCN2 is also required for UV light-induced translation inhibition, and in vivo phosphorylation of murine GCN2 at Thr898 is induced by both UV irradiation and by leucine deprivation (3). UV-induced activation of NF-κB also requires GCN2, which may act simply by preventing translation of IκB-alpha to replace pools that have been ubiquitinated and degraded (4). Interestingly, proteasome inhibitors (MG132 and ALLN) activate the GCN2/eIF2alpha pathway, suggesting a pivotal role for this kinase in stress response and ubiquitin-mediated signaling (5). In vitro autophosphorylation of yeast GCN2 within its activation loop at Thr882 and Thr887 (Thr898 and Thr903 in mouse) has also been reported (6).
- Kaufman, R.J. (1999) Genes Dev 13, 1211-33.
- Sheikh, M.S. and Fornace, A.J. (1999) Oncogene 18, 6121-8.
- Deng, J. et al. (2002) Curr Biol 12, 1279-86.
- Jiang, H.Y. and Wek, R.C. (2005) Biochem J 385, 371-80.
- Jiang, H.Y. and Wek, R.C. (2005) J Biol Chem 280, 14189-202.
- Garcia-Barrio, M. et al. (2002) J Biol Chem 277, 30675-83.
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