Reduced eIF2α phosphorylation and increased proapoptotic proteins in aging

Biochemical and Biophysical Research Communications

Volumn 355, Issue 2, 2007, Pages 365-370

  Hussain, Syed G ^a   Ramaiah, Kolluru V A ^a  

^a UNIVERSITY OF HYDERABAD   (India)

Author keywords

Aging; ATF4; BiP; CHOP; eIF2 phosphorylation; ER stress; GADD 34; Translation

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR 2ALPHA; PROTEIN; PROTEIN GADD34; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; ATF4 PROTEIN, RAT; CHAPERONE; HEAT SHOCK PROTEIN; HSPA5 PROTEIN, RAT; INITIATION FACTOR 2;

AGING; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; APOPTOSIS; ARTICLE; ENDOPLASMIC RETICULUM; ENZYME ANALYSIS; GENE EXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; RAT; TISSUE DISTRIBUTION; ANIMAL; METABOLISM; PHOSPHORYLATION; SIGNAL TRANSDUCTION;

EUKARYOTA; RATTUS;

ACTIVATING TRANSCRIPTION FACTOR 4; AGING; ANIMALS; APOPTOSIS; EUKARYOTIC INITIATION FACTOR-2; HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PHOSPHORYLATION; RATS; SIGNAL TRANSDUCTION;

EID: 33847149663     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.01.156     Document Type: Article

References (33)

1. Lee C.K., Allison D.B., Brand J., Weindruch R., and Prolla T.A. Transcriptional profiles associated with aging and middle age-onset caloric restriction in mouse hearts. Proc. Natl. Acad. Sci. USA 99 (2002) 14988-14993
2. Rhoads R.E. Signal transduction pathways that regulate eukaryotic protein synthesis. J. Biol. Chem. 274 (1999) 30337-30340
3. Hinnebusch A.G., Asano K., Olsen D.S., Phan L., Nielsen K.H., and Valasek L. Study of translational control of eukaryotic gene expression using yeast. Ann. N.Y. Acad. Sci. 1038 (2004) 60-74
4. Dever T.E. Gene-specific regulation by general translation factors. Cell 108 (2002) 545-556
5. Gebauer F., and Hentze M.W. Molecular mechanisms of translational control. Mol. Cell. Biol. (2004) 827-835
6. Raught B., Gingras A., and Sonenberg N. The target of rapamycin (TOR) proteins. Proc. Natl. Acad. Sci. USA (2001) 7037-7044
7. Sudhakar A., Ramachandran A., Ghosh S., Hasnain S.E., Kaufman R.J., and Ramaiah K.V.A. Phosphorylation of serine 51 in initiation factor 2 alpha (eIF2 alpha) promotes complex formation between eIF2 alpha(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B. Biochemistry 39 (2000) 12929-12938
8. Scheuner D., Song B., McEwen E., Liu C., Laybutt R., Gillespie P., Saunders T., Bonner-Weir S., and Kaufman R.J. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol. Cell 7 (2001) 1165-1176
9. Scheuner D., Patel R., Wang F., Lee K., Kumar K., Wu J., Nilsson A., Karin M., and Kaufman R.J. Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis. J. Biol. Chem. 281 (2006) 21458-21468
10. Harding H., Zhang Y., Bertolotti A., Zeng H., and Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5 (2000) 897-904
11. Thulasiraman V., Xu Z., Uma S., Gu Y., Chen J.J., and Matts R.L. Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIF-2alpha kinase in rabbit reticulocyte lysate. Eur. J. Biochem. 255 (1998) 552-562
12. Zhang P., McGrath B.C., Reinert J., Olsen D.S., Lei L., Gill S.A., Wek K., Vattem K., Wek R.C., and Kimball S.R. The GCN2 eIF2alpha kinase is required for adaptation to amino acid deprivation in mice. Mol. Cell. Biol. 22 (2002) 6681-6688
13. Tan S., Somia N., Maher P., and Schubert D. Regulation of antioxidant metabolism by translation initiation factor 2 alpha. J. Cell Biol. 152 (2001) 997-1006
14. 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., and Ron D. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11 (2003) 619-633
15. Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., and Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6 (2000) 1099-1108
16. Holcik M., and Sonenberg N. Translational control in stress and apoptosis. Nat. Rev. Mol. Cell. Biol. 6 (2005) 318-327
17. Brush M.H., Weiser D.C., and Shenolikar S. Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Mol. Cell. Biol. 23 (2003) 1292-1303
18. Novoa I., Zenga H., Harding H.P., and Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2. J. Cell Biol. 153 (2001) 1011-1022
19. Szegezdi E., Logue S.E., Gorman A.M., and Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep. 7 (2006) 880-885
20. Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., and Yuan J. A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 307 (2005) 935-939
21. Holbrook N.J., and Ikeyama S. Age-related decline in cellular response to oxidative stress: links to growth factor signaling pathways with common defects. Biochem. Pharmacol. 64 (2002) 999-1005
22. Hall D.M., Xu L., Drake V.J., Oberley L.W., Oberley T.D., Moseley P.L., and Kregel K.C. Aging reduces adaptive capacity and stress protein expression in the liver after heat stress. J. Appl. Physiol. 89 (2000) 749-759
23. Li J., and Holbrook N.J. Elevated gadd153/chop expression and enhanced c-Jun N-terminal protein kinase activation sensitizes aged cells to ER stress. Exp. Gerontol. 39 (2004) 735-744
24. Ikeyama S., Wang X.T., Li J., Podlutsky A., Martindale J.L., Kokkonen G., van Huizen R., Gorospe M., and Holbrook N.J. Expression of the pro-apoptotic gene gadd153/chop is elevated in liver with aging and sensitizes cells to oxidant injury. J. Biol. Chem. 278 (2003) 16726-16731
25. Kimball S.R., Vary T.C., and Jefferson L.S. Age-dependent decrease in the amount of eukaryotic initiation factor 2 in various rat tissues. Biochem. J. 286 (1992) 263-268
26. Fernandez J., Yaman I., Sarnow P., Snider M.D., and Hatzoglou M. Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2alpha. J. Biol. Chem. 277 (2002) 19198-19205
27. Ladiges W., Morton J., Blakely C., and Gale M. Tissue specific expression of PKR protein kinase in aging B6D2F1 mice. Mech. Ageing Dev. 114 (2000) 123-132
28. Bartsch D., Ghirardi M., Skehel P.A., Karl K.A., Herder S.P., Chen M., Bailey C.H., and Kandel E.R. Aplysia CREB2 represses long-term facilitation: relief of repression converts transient facilitation into long-term functional and structural change. Cell 83 (1995) 979-992
29. Hendershot L.M. The ER chaperone BiP is a master regulator of ER function. Mt. Sinai J. Med. 71 (2004) 289-297
30. Zhang K., and Kaufman R.J. Signaling the unfolded protein response from the endoplasmic reticulum. J. Biol. Chem. 279 (2004) 25935-25938
31. Gulow K., Bienert D., and Hass I.G. BiP is feed-back regulated by control of protein translation efficiency. J. Cell. Sci. 115 (2002) 2443-2452
32. Luo S., Baumeister P., Yang S., Abcouwer S.F., and Lee A.S. Induction of GRP78/BiP by translational block. J. Biol. Chem. 278 (2003) 37375-37385
33. Marciniak S.J., Yun C., Oyadomari S., Novoa I., Zhang Y., Jungreis R., Nagata K., Harding H.P., and Ron D. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev. 18 (2004) 3066-3077