Gene Review:
Eif2s1 - eukaryotic translation initiation factor 2...
Mus musculus
Synonyms:
0910001O23Rik, 2410026C18Rik, 35kDa, Eif2a, Eukaryotic translation initiation factor 2 subunit 1, ...
- Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Scheuner, D., Song, B., McEwen, E., Liu, C., Laybutt, R., Gillespie, P., Saunders, T., Bonner-Weir, S., Kaufman, R.J. Mol. Cell (2001)
- Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. Novoa, I., Zeng, H., Harding, H.P., Ron, D. J. Cell Biol. (2001)
- Importance of eIF2alpha phosphorylation and stress granule assembly in alphavirus translation regulation. McInerney, G.M., Kedersha, N.L., Kaufman, R.J., Anderson, P., Liljeström, P. Mol. Biol. Cell (2005)
- PERK is responsible for the increased phosphorylation of eIF2alpha and the severe inhibition of protein synthesis after transient global brain ischemia. Owen, C.R., Kumar, R., Zhang, P., McGrath, B.C., Cavener, D.R., Krause, G.S. J. Neurochem. (2005)
- Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR. Dar, A.C., Dever, T.E., Sicheri, F. Cell (2005)
- Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Scheuner, D., Mierde, D.V., Song, B., Flamez, D., Creemers, J.W., Tsukamoto, K., Ribick, M., Schuit, F.C., Kaufman, R.J. Nat. Med. (2005)
- Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Harding, H.P., Zhang, Y., Ron, D. Nature (1999)
- Phosphorylation of the alpha subunit of translation initiation factor-2 by PKR mediates protein synthesis inhibition in the mouse brain during status epilepticus. Carnevalli, L.S., Pereira, C.M., Jaqueta, C.B., Alves, V.S., Paiva, V.N., Vattem, K.M., Wek, R.C., Mello, L.E., Castilho, B.A. Biochem. J. (2006)
- CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Marciniak, S.J., Yun, C.Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H.P., Ron, D. Genes Dev. (2004)
- Oxidative injury to the endoplasmic reticulum in mouse brains after transient focal ischemia. Hayashi, T., Saito, A., Okuno, S., Ferrand-Drake, M., Dodd, R.L., Chan, P.H. Neurobiol. Dis. (2004)
- Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses. Jiang, H.Y., Wek, S.A., McGrath, B.C., Scheuner, D., Kaufman, R.J., Cavener, D.R., Wek, R.C. Mol. Cell. Biol. (2003)
- IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1 and inhibits GCN2 activation. Pereira, C.M., Sattlegger, E., Jiang, H.Y., Longo, B.M., Jaqueta, C.B., Hinnebusch, A.G., Wek, R.C., Mello, L.E., Castilho, B.A. J. Biol. Chem. (2005)
- Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. Ma, Y., Hendershot, L.M. J. Biol. Chem. (2003)
- Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition. Jiang, H.Y., Wek, R.C. J. Biol. Chem. (2005)
- Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase. Berlanga, J.J., Santoyo, J., De Haro, C. Eur. J. Biochem. (1999)
- Cloning of hHRI, human heme-regulated eukaryotic initiation factor 2alpha kinase: down-regulated in epithelial ovarian cancers. Hwang, S.Y., Kim, M.K., Kim, J.C. Mol. Cells (2000)
- RNA CUG-binding protein 1 increases translation of 20-kDa isoform of CCAAT/enhancer-binding protein beta by interacting with the alpha and beta subunits of eukaryotic initiation translation factor 2. Timchenko, N.A., Wang, G.L., Timchenko, L.T. J. Biol. Chem. (2005)
- AMPK activation regulates apoptosis, adipogenesis, and lipolysis by eIF2alpha in adipocytes. Dagon, Y., Avraham, Y., Berry, E.M. Biochem. Biophys. Res. Commun. (2006)
- Basal levels of eIF2alpha phosphorylation determine cellular antioxidant status by regulating ATF4 and xCT expression. Lewerenz, J., Maher, P. J. Biol. Chem. (2009)
- Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Deng, J., Lu, P.D., Zhang, Y., Scheuner, D., Kaufman, R.J., Sonenberg, N., Harding, H.P., Ron, D. Mol. Cell. Biol. (2004)
- A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha. Sood, R., Porter, A.C., Olsen, D.A., Cavener, D.R., Wek, R.C. Genetics (2000)
- The double-stranded RNA-activated protein kinase PKR is dispensable for regulation of translation initiation in response to either calcium mobilization from the endoplasmic reticulum or essential amino acid starvation. Kimball, S.R., Clemens, M.J., Tilleray, V.J., Wek, R.C., Horetsky, R.L., Jefferson, L.S. Biochem. Biophys. Res. Commun. (2001)
- Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells. Jousse, C., Oyadomari, S., Novoa, I., Lu, P., Zhang, Y., Harding, H.P., Ron, D. J. Cell Biol. (2003)
- An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Harding, H.P., Zhang, Y., Zeng, H., Novoa, I., Lu, P.D., Calfon, M., Sadri, N., Yun, C., Popko, B., Paules, R., Stojdl, D.F., Bell, J.C., Hettmann, T., Leiden, J.M., Ron, D. Mol. Cell (2003)
- Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection. Balachandran, S., Roberts, P.C., Brown, L.E., Truong, H., Pattnaik, A.K., Archer, D.R., Barber, G.N. Immunity (2000)
- Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis. Scheuner, D., Patel, R., Wang, F., Lee, K., Kumar, K., Wu, J., Nilsson, A., Karin, M., Kaufman, R.J. J. Biol. Chem. (2006)
- Changes in the phosphorylation of initiation factor eIF-2alpha, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice. Althausen, S., Mengesdorf, T., Mies, G., Oláh, L., Nairn, A.C., Proud, C.G., Paschen, W. J. Neurochem. (2001)