EIF5 has GDI activity necessary for translational control by eIF2 phosphorylation

Nature

Volumn 465, Issue 7296, 2010, Pages 378-381

  Jennings, Martin D ^a   Pavitt, Graham D ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ARGONAUTE 2 PROTEIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; MESSENGER RNA; TRANSCRIPTION FACTOR GCN4;

BIOCHEMISTRY; CYTOLOGY; EUKARYOTE; NUCLEIC ACID; PROTEIN;

ALLELE; ARTICLE; CELL CULTURE; CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME REGULATION; ESCHERICHIA COLI; GENE OVEREXPRESSION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN MALNUTRITION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN SYNTHESIS; RESIDUE ANALYSIS; TRANSLATION INITIATION; WILD TYPE; YEAST;

BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; EUKARYOTIC INITIATION FACTOR-2; GTPASE-ACTIVATING PROTEINS; GUANINE NUCLEOTIDE DISSOCIATION INHIBITORS; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PEPTIDE CHAIN INITIATION, TRANSLATIONAL; PEPTIDE INITIATION FACTORS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN SUBUNITS; RNA, TRANSFER, MET; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA;

EID: 77952734403     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09003     Document Type: Article

References (29)

1. Kapp, L. D. & Lorsch, J. R. The molecular mechanics of eukaryotic translation. Annu. Rev. Biochem. 73, 657-704 (2004).
2. Sonenberg, N. & Hinnebusch, A. G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136, 731-745 (2009).
3. Scheuner, D. et al. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Nature Med. 11, 757-764 (2005). (Pubitemid 41021208)
4. Costa-Mattioli, M. et al. eIF2a phosphorylation bidirectionally regulates the switch from short-to long-term synaptic plasticity and memory. Cell 129, 195-206 (2007). (Pubitemid 46507591)
5. Mohr, I. Neutralizing innate host defenses to control viral translation in HSV-1 infected cells. Int. Rev. Immunol. 23, 199-220 (2004). (Pubitemid 38121753)
6. i release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 20, 251-262 (2005). (Pubitemid 41484170)
7. Das, S., Ghosh, R. & Maitra, U. Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein. J. Biol. Chem. 276, 6720-6726 (2001). (Pubitemid 37373537)
8. Paulin, F. E. et al. Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein. Curr. Biol. 11, 55-59 (2001). (Pubitemid 32062717)
9. Cheung, Y. N. et al. Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo. Genes Dev. 21, 1217-1230 (2007).
10. Unbehaun, A., Borukhov, S. I., Hellen, C. U. & Pestova, T. V. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev. 18, 3078-3093 (2004). (Pubitemid 39658176)
11. Singh, C. R. et al. An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J. 25, 4537-4546 (2006).
12. DerMardirossian, C. & Bokoch, G. M. GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15, 356-363 (2005).
13. Pavitt, G. D., Ramaiah, K. V., Kimball, S. R. & Hinnebusch, A. G. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev. 12, 514-526 (1998).
14. Schmitt, E., Blanquet, S. & Mechulam, Y. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21, 1821-1832 (2002). (Pubitemid 34614638)
15. Asano, K. et al. Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18, 1673-1688 (1999). (Pubitemid 29127079)
16. Asano, K. et al. Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J. 20, 2326-2337 (2001). (Pubitemid 32410601)
17. Conte, M. R. et al. Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry 45, 4550-4558 (2006).
18. Wei, Z., Xue, Y., Xu, H. & Gong, W. Crystal structure of the C-terminal domain of S. cerevisiae eIF5. J. Mol. Biol. 359, 1-9 (2006).
19. Alone, P. V. & Dever, T. E. Direct binding of translation initiation factor eIF2c-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2Be. J. Biol. Chem. 281, 12636-12644 (2006).
20. Hinnebusch, A. G. Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59, 407-450 (2005).
21. Singh, C. R. et al. Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation. Mol. Cell. Biol. 25, 5480-5491 (2005).
22. Ramirez, M. et al. Mutations activating the yeast eIF-2a kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. Mol. Cell. Biol. 12, 5801-5815 (1992).
23. Pavitt, G. D., Yang, W. & Hinnebusch, A. G. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol. 17, 1298-1313 (1997). (Pubitemid 27097359)
24. Met ternary complexes. Mol. Cell. Biol. 15, 6351-6363 (1995).
25. Krishnamoorthy, T. et al. Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2a) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol. Cell. Biol. 21, 5018-5030 (2001). (Pubitemid 32656399)
26. Mohammad-Qureshi, S. S. et al. Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2b and-2c mediate guanine nucleotide exchange. Mol. Cell. Biol. 27, 5225-5234 (2007).
27. Adams, A., Gottschling, D. E., Kaiser, C. A. & Stearns, T. Methods in Yeast genetics: A Cold Spring Harbor Laboratory Course Manual (Cold Spring Harbor Laboratory Press, 1998).
28. Gietz, R. D. & Woods, R. A. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350, 87-96 (2002).
29. Phan, L. et al. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol. 18, 4935-4946 (1998). (Pubitemid 28343076)