The many roles of the eukaryotic elongation factor 1 complex

Advanced Review

Arjun N. Sasikumar, Winder B. Perez, Terri Goss Kinzy

Published Online: May 03 2012

DOI: 10.1002/wrna.1118

Full article on Wiley Online Library: HTML PDF

Can't access this content? Tell your librarian.

Abstract The vast majority of proteins are believed to have one specific function. Throughout the course of evolution, however, some proteins have acquired additional functions to meet the demands of a complex cellular milieu. In some cases, changes in RNA or protein processing allow the cell to make the most of what is already encoded in the genome to produce slightly different forms. The eukaryotic elongation factor 1 (eEF1) complex subunits, however, have acquired such moonlighting functions without alternative forms. In this article, we discuss the canonical functions of the components of the eEF1 complex in translation elongation as well as the secondary interactions they have with other cellular factors outside of the translational apparatus. The eEF1 complex itself changes in composition as the complexity of eukaryotic organisms increases. Members of the complex are also subject to phosphorylation, a potential modulator of both canonical and non‐canonical functions. Although alternative functions of the eEF1A subunit have been widely reported, recent studies are shedding light on additional functions of the eEF1B subunits. A thorough understanding of these alternate functions of eEF1 is essential for appreciating their biological relevance. WIREs RNA 2012, 3:543–555. doi: 10.1002/wrna.1118 This article is categorized under: Translation > Translation Mechanisms Translation > Translation Regulation

Model of eukaryotic elongation factor 1 (eEF1) complex. The variation in the organization of the eEF1 complex in different organisms illustrates the differences in the composition as well as the interactions of the various subunits. Domain I, the largest domain of eEF1A (gold) is the GTP‐binding domain. For the eEF1B subunits α (red) γ (blue) δ (green), the N‐ and C‐terminal domains are indicated in darker and lighter shades, respectively. Valyl tRNA synthetase (Val‐RS; purple) interacts with the eEF1 complex in metazoans.

[ Normal View | Magnified View ]

The role of eukaryotic elongation factor 1 (eEF1A) in minus‐strand synthesis of positive‐strand viral RNAs. Upon release of the viral RNA (green) into the cytoplasm, eEF1A (yellow) binds at the tRNA‐like structure at the 3′‐end of the RNA preventing the RNA‐dependent RNA polymerase (RdRp, blue) from initiating minus‐strand synthesis. By inhibiting minus‐strand synthesis, eEF1A allows viral proteins to be synthesized first. Once sufficient RdRp is made, RdRp competes eEF1A off of the viral end allowing for minus‐strand synthesis to occur.

[ Normal View | Magnified View ]

Location of mutations that affect non‐canonical functions and known phosphorylation sites on eukaryotic elongation factor 1A (eEF1A). eEF1A from Saccharomyces cerevisiae is composed of three well‐defined domains as determined from the co‐crystal structure with the C‐terminus of eEF1Bα. Domain I (blue) binds GTP, domain II (red) is proposed to interact with the aminoacyl end of the aa‐tRNA, and domains II and III (green) are linked to actin binding and bundling. eEF1Bα binds eEF1A in domains I and II. Colored spheres indicate mutations that affect the non‐canonical functions of eEF1A. In domain I, Asp156Asn (purple) affects protein turnover. In domain II, Glu286Lys and Glu291Lys (cyan) affect nuclear transport. Mutations that affect actin organization, Asn305Ser, Asn329Ser, Phe308Lys, and Ser405Pro (yellow), are shown in domains II and III. Phosphorylation of Glu298 (the yeast equivalent of human Ser300) (orange) may lead to downregulation of translation. The figure was prepared with PyMol using Protein Data Bank 1F60.43

[ Normal View | Magnified View ]

References

Le Sourd, F, Boulben, S, Le Bouffant, R, Cormier, P, Morales, J, Belle, R, Mulner‐Lorillon, O. eEF1B: at the dawn of the 21st century. Biochim Biophys Acta 2006, 1759:13–31.
Sang Lee, J, Gyu Park, S, Park, H, Seol, W, Lee, S, Kim, S. Interaction network of human aminoacyl‐tRNA synthetases and subunits of elongation factor 1 complex. Biochem Biophys Res Commun 2002, 291:158–164.
Carvalho, MD, Carvalho, JF, Merrick, WC. Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes. Arch Biochem Biophys 1984, 234:603–611.
Taylor, DR, Frank, J, Kinzy, TG. Structure and function of the eukaryotic ribosome and elongation factors. In: Sonenberg, N, Hershey, JWB, Mathews, MB, eds. Translational Control in Biology and Medicine. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 2007, 59–85.
Pittman, YR, Valente, L, Jeppesen, MG, Andersen, GR, Patel, S, Kinzy, TG. Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha. J Biol Chem 2006, 281:19457–19468.
Janssen, GM, Moller, W. Kinetic studies on the role of elongation factors 1 beta and 1 gamma in protein synthesis. J Biol Chem 1988, 263:1773–1778.
Jeppesen, MG, Ortiz, P, Shepard, W, Kinzy, TG, Nyborg, J, Andersen, GR. The crystal structure of the glutathione S‐transferase‐like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae. J Biol Chem 2003, 278:47190–47198.
Kinzy, TG, Ripmaster, TL, Woolford, JL Jr. Multiple genes encode the translation elongation factor EF‐1 gamma in Saccharomyces cerevisiae. Nucleic Acids Res 1994, 22:2703–2707.
Sanders, J, Brandsma, M, Janssen, GM, Dijk, J, Moller, W. Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor‐1 beta gamma delta in the endoplasmic reticulum. J Cell Sci 1996, 109(pt 5):1113–1117.
Bec, G, Kerjan, P, Waller, JP. Reconstitution in vitro of the valyl‐tRNA synthetase‐elongation factor (EF) 1 beta gamma delta complex. Essential roles of the NH2‐terminal extension of valyl‐tRNA synthetase and of the EF‐1 delta subunit in complex formation. J Biol Chem 1994, 269:2086–2092.
Negrutskii, BS, Stapulionis, R, Deutscher, MP. Supramolecular organization of the mammalian translation system. Proc Natl Acad Sci U S A 1994, 91:964–968.
Peters, HI, Chang, YW, Traugh, JA. Phosphorylation of elongation factor 1 (EF‐1) by protein kinase C stimulates GDP/GTP‐exchange activity. Eur J Biochem 1995, 234:550–556.
Venema, RC, Peters, HI, Traugh, JA. Phosphorylation of valyl‐tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities. J Biol Chem 1991, 266:11993–11998.
Chang, YW, Traugh, JA. Insulin stimulation of phosphorylation of elongation factor 1 (eEF‐1) enhances elongation activity. Eur J Biochem 1998, 251:201–207.
Janssen, GM, Morales, J, Schipper, A, Labbe, JC, Mulner‐Lorillon, O, Belle, R, Moller, W. A major substrate of maturation promoting factor identified as elongation factor 1 beta gamma delta in Xenopus laevis. J Biol Chem 1991, 266:14885–14888.
Mulner‐Lorillon, O, Minella, O, Cormier, P, Capony, JP, Cavadore, JC, Morales, J, Poulhe, R, Belle, R. Elongation factor EF‐1 delta, a new target for maturation‐promoting factor in Xenopus oocytes. J Biol Chem 1994, 269:20201–20207.
Sivan, G, Aviner, R, Elroy‐Stein, O. Mitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes. J Biol Chem 2011, 286:27927–27935.
Sheu, GT, Traugh, JA. A structural model for elongation factor 1 (EF‐1) and phosphorylation by protein kinase CKII. Mol Cell Biochem 1999, 191:181–186.
Lin, KW, Yakymovych, I, Jia, M, Yakymovych, M, Souchelnytskyi, S. Phosphorylation of eEF1A1 at Ser300 by TbetaR‐I results in inhibition of mRNA translation. Curr Biol 2010, 20:1615–1625.
Lamberti, A, Longo, O, Marra, M, Tagliaferri, P, Bismuto, E, Fiengo, A, Viscomi, C, Budillon, A, Rapp, UR, Wang, E, et al. C‐Raf antagonizes apoptosis induced by IFN‐alpha in human lung cancer cells by phosphorylation and increase of the intracellular content of elongation factor 1A. Cell Death Differ 2007, 14:952–962.
Eckhardt, K, Troger, J, Reissmann, J, Katschinski, DM, Wagner, KF, Stengel, P, Paasch, U, Hunziker, P, Borter, E, Barth, S, et al. Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1. Cell Physiol Biochem 2007, 20:227–240.
Fan, Y, Schlierf, M, Gaspar, AC, Dreux, C, Kpebe, A, Chaney, L, Mathieu, A, Hitte, C, Gremy, O, Sarot, E, et al. Drosophila translational elongation factor‐1gamma is modified in response to DOA kinase activity and is essential for cellular viability. Genetics 2010, 184:141–154.
Pomerening, JR, Valente, L, Kinzy, TG, Jacobs, TW. Mutation of a conserved CDK site converts a metazoan elongation factor 1Bbeta subunit into a replacement for yeast eEF1Balpha. Mol Genet Genomics 2003, 269:776–788.
Boulben, S, Monnier, A, Le Breton, M, Morales, J, Cormier, P, Belle, R, Mulner‐Lorillon, O. Sea urchin elongation factor 1delta (EF1delta) and evidence for cell cycle‐directed localization changes of a sub‐fraction of the protein at M phase. Cell Mol Life Sci 2003, 60:2178–2188.
Tanaka, TS, Nishiumi, F, Komiya, T, Ikenishi, K. Characterization of the 38 kDa protein lacking in gastrula‐arrested mutant Xenopus embryos. Int J Dev Biol 2010, 54:1347–1353.
Kawaguchi, Y, Kato, K, Tanaka, M, Kanamori, M, Nishiyama, Y, Yamanashi, Y. Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1delta. J Virol 2003, 77:2359–2368.
Moon, HM, Redfield, B, Millard, S, Vane, F, Weissbach, H. Multiple forms of elongation factor 1 from calf brain. Proc Natl Acad Sci U S A 1973, 70:3282–3286.
Legocki, AB, Redfield, B, Liu, CK, Weissbach, H. Role of phospholipids in the multiple forms of mammalian elongation factor 1. Proc Natl Acad Sci U S A 1974, 71:2179–2182.
Janssen, GM, van Damme, HT, Kriek, J, Amons, R, Moller, W. The subunit structure of elongation factor 1 from Artemia. Why two alpha‐chains in this complex? J Biol Chem 1994, 269:31410–31417.
Mansilla, F, Friis, I, Jadidi, M, Nielsen, KM, Clark, BF, Knudsen, CR. Mapping the human translation elongation factor eEF1H complex using the yeast two‐hybrid system. Biochem J 2002, 365:669–676.
Jiang, S, Wolfe, CL, Warrington, JA, Norcum, MT. Three‐dimensional reconstruction of the valyl‐tRNA synthetase/elongation factor‐1H complex and localization of the delta subunit. FEBS Lett 2005, 579:6049–6054.
Ong, LL, Er, CP, Ho, A, Aung, MT, Yu, H. Kinectin anchors the translation elongation factor‐1 delta to the endoplasmic reticulum. J Biol Chem 2003, 278:32115–32123.
Ong, LL, Lin, PC, Zhang, X, Chia, SM, Yu, H. Kinectin‐dependent assembly of translation elongation factor‐1 complex on endoplasmic reticulum regulates protein synthesis. J Biol Chem 2006, 281:33621–33634.
Stapulionis, R, Kolli, S, Deutscher, MP. Efficient mammalian protein synthesis requires an intact F‐actin system. J Biol Chem 1997, 272:24980–24986.
Yang, F, Demma, M, Warren, V, Dharmawardhane, S, Condeelis, J. Identification of an actin‐binding protein from Dictyostelium as elongation factor 1a. Nature 1990, 347:494–496.
Liu, G, Tang, J, Edmonds, BT, Murray, J, Levin, S, Condeelis, J. F‐actin sequesters elongation factor 1alpha from interaction with aminoacyl‐tRNA in a pH‐dependent reaction. J Cell Biol 1996, 135:953–963.
Murray, JW, Edmonds, BT, Liu, G, Condeelis, J. Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends. J Cell Biol 1996, 135:1309–1321.
Winkler, MM, Steinhardt, RA, Grainger, JL, Minning, L. Dual ionic controls for the activation of protein synthesis at fertilization. Nature 1980, 287:558–560.
Munshi, R, Kandl, KA, Carr‐Schmid, A, Whitacre, JL, Adams, AE, Kinzy, TG. Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast. Genetics 2001, 157:1425–1436.
Gross, SR, Kinzy, TG. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat Struct Mol Biol 2005, 12:772–778.
Gross, SR, Kinzy, TG. Improper organization of the actin cytoskeleton affects protein synthesis at initiation. Mol Cell Biol 2007, 27:1974–1989.
Umikawa, M, Tanaka, K, Kamei, T, Shimizu, K, Imamura, H, Sasaki, T, Takai, Y. Interaction of Rho1p target Bni1p with F‐actin‐binding elongation factor 1alpha: implication in Rho1p‐regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene 1998, 16:2011–2016.
Andersen, GR, Pedersen, L, Valente, L, Chatterjee, I, Kinzy, TG, Kjeldgaard, M, Nyborg, J. Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Mol Cell 2000, 6:1261–1266.
Ohta, K, Toriyama, M, Miyazaki, M, Murofushi, H, Hosoda, S, Endo, S, Sakai, H. The mitotic apparatus‐associated 51‐kDa protein from sea urchin eggs is a GTP‐binding protein and is immunologically related to yeast polypeptide elongation factor 1 alpha. J Biol Chem 1990, 265:3240–3247.
Durso, NA, Cyr, RJ. A calmodulin‐sensitive interaction between microtubules and a higher plant homolog of elongation factor‐1 alpha. Plant Cell 1994, 6:893–905.
Moore, RC, Durso, NA, Cyr, RJ. Elongation factor‐1alpha stabilizes microtubules in a calcium/calmodulin‐dependent manner. Cell Motil Cytoskeleton 1998, 41:168–180.
Shiina, N, Gotoh, Y, Kubomura, N, Iwamatsu, A, Nishida, E. Microtubule severing by elongation factor 1 alpha. Science 1994, 266:282–285.
Moore, RC, Cyr, RJ. Association between elongation factor‐1alpha and microtubules in vivo is domain dependent and conditional. Cell Motil Cytoskeleton 2000, 45:279–292.
Pedersen, L, Andersen, GR, Knudsen, CR, Kinzy, TG, Nyborg, J. Crystallization of the yeast elongation factor complex eEF1A‐eEF1B alpha. Acta Crystallogr D Biol Crystallogr 2001, 57:159–161.
Furukawa, R, Jinks, TM, Tishgarten, T, Mazzawi, M, Morris, DR, Fechheimer, M. Elongation factor 1beta is an actin‐binding protein. Biochim Biophys Acta 2001, 1527:130–140.
Pittman, YR, Kandl, K, Lewis, M, Valente, L, Kinzy, TG. Coordination of eukaryotic translation elongation factor 1A (eEF1A) function in actin organization and translation elongation by the guanine nucleotide exchange factor eEF1Balpha. J Biol Chem 2009, 284:4739–4747.
Kim, S, Wong, P, Coulombe, PA. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature 2006, 441:362–365.
Kim, S, Kellner, J, Lee, CH, Coulombe, PA. Interaction between the keratin cytoskeleton and eEF1Bgamma affects protein synthesis in epithelial cells. Nat Struct Mol Biol 2007, 14:982–983.
Kim, S, Coulombe, PA. Emerging role for the cytoskeleton as an organizer and regulator of translation. Nat Rev Mol Cell Biol 2010, 11:75–81.
Howe, JG, Hershey, JW. Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells. Cell 1984, 37:85–93.
Vedeler, A, Pryme, IF, Hesketh, JE. The characterization of free, cytoskeletal and membrane‐bound polysomes in Krebs II ascites and 3T3 cells. Mol Cell Biochem 1991, 100:183–193.
Grosshans, H, Hurt, E, Simos, G. An aminoacylation‐dependent nuclear tRNA export pathway in yeast. Genes Dev 2000, 14:830–840.
Grosshans, H, Simos, G, Hurt, E. Review: transport of tRNA out of the nucleus‐direct channeling to the ribosome? J Struct Biol 2000, 129:288–294.
Shaheen, HH, Hopper, AK. Retrograde movement of tRNAs from the cytoplasm to the nucleus in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 2005, 102:11290–11295.
Bohnsack, MT, Regener, K, Schwappach, B, Saffrich, R, Paraskeva, E, Hartmann, E, Gorlich, D. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J 2002, 21:6205–6215.
Calado, A, Treichel, N, Muller, EC, Otto, A, Kutay, U. Exportin‐5‐mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J 2002, 21:6216–6224.
Murthi, A, Shaheen, HH, Huang, HY, Preston, MA, Lai, TP, Phizicky, EM, Hopper, AK. Regulation of tRNA bidirectional nuclear‐cytoplasmic trafficking in Saccharomyces cerevisiae. Mol Biol Cell 2010, 21:639–649.
Gonen, H, Smith, CE, Siegel, NR, Kahana, C, Merrick, WC, Chakraburtty, K, Schwartz, AL, Ciechanover, A. Protein synthesis elongation factor EF‐1 alpha is essential for ubiquitin‐dependent degradation of certain N alpha‐acetylated proteins and may be substituted for by the bacterial elongation factor EF‐Tu. Proc Natl Acad Sci U S A 1994, 91:7648–7652.
Hotokezaka, Y, Tobben, U, Hotokezaka, H, Van Leyen, K, Beatrix, B, Smith, DH, Nakamura, T, Wiedmann, M. Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides. J Biol Chem 2002, 277:18545–18551.
Caldas, TD, El Yaagoubi, A, Richarme, G. Chaperone properties of bacterial elongation factor EF‐Tu. J Biol Chem 1998, 273:11478–11482.
Chuang, SM, Chen, L, Lambertson, D, Anand, M, Kinzy, TG, Madura, K. Proteasome‐mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol Cell Biol 2005, 25:403–413.
Duttaroy, A, Bourbeau, D, Wang, XL, Wang, E. Apoptosis rate can be accelerated or decelerated by overexpression or reduction of the level of elongation factor‐1 alpha. Exp Cell Res 1998, 238:168–176.
Talapatra, S, Wagner, JD, Thompson, CB. Elongation factor‐1 alpha is a selective regulator of growth factor withdrawal and ER stress‐induced apoptosis. Cell Death Differ 2002, 9:856–861.
Kahns, S, Lund, A, Kristensen, P, Knudsen, CR, Clark, BF, Cavallius, J, Merrick, WC. The elongation factor 1 A‐2 isoform from rabbit: cloning of the cDNA and characterization of the protein. Nucleic Acids Res 1998, 26:1884–1890.
Lee, S, Francoeur, AM, Liu, S, Wang, E. Tissue‐specific expression in mammalian brain, heart, and muscle of S1, a member of the elongation factor‐1 alpha gene family. J Biol Chem 1992, 267:24064–24068.
Ruest, LB, Marcotte, R, Wang, E. Peptide elongation factor eEF1A‐2/S1 expression in cultured differentiated myotubes and its protective effect against caspase‐3‐mediated apoptosis. J Biol Chem 2002, 277:5418–5425.
De Nova‐Ocampo, M, Villegas‐Sepulveda, N, del Angel, RM. Translation elongation factor‐1alpha, La, and PTB interact with the 3′ untranslated region of dengue 4 virus RNA. Virology 2002, 295:337–347.
Matsuda, D, Yoshinari, S, Dreher, TW. eEF1A binding to aminoacylated viral RNA represses minus strand synthesis by TYMV RNA‐dependent RNA polymerase. Virology 2004, 321:47–56.
Yamaji, Y, Kobayashi, T, Hamada, K, Sakurai, K, Yoshii, A, Suzuki, M, Namba, S, Hibi, T. In vivo interaction between Tobacco mosaic virus RNA‐dependent RNA polymerase and host translation elongation factor 1A. Virology 2006, 347:100–108.
Li, Z, Pogany, J, Tupman, S, Esposito, AM, Kinzy, TG, Nagy, PD. Translation elongation factor 1A facilitates the assembly of the tombusvirus replicase and stimulates minus‐strand synthesis. PLoS Pathog 2010, 6:e1001175.
Blackwell, JL, Brinton, MA. Translation elongation factor‐1 alpha interacts with the 3′ stem‐loop region of West Nile virus genomic RNA. J Virol 1997, 71:6433–6444.
Dreher, TW, Goodwin, JB. Transfer RNA mimicry among tymoviral genomic RNAs ranges from highly efficient to vestigial. Nucleic Acids Res 1998, 26:4356–4364.
Das, T, Mathur, M, Gupta, AK, Janssen, GM, Banerjee, AK. RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor‐1 alphabetagamma for its activity. Proc Natl Acad Sci U S A 1998, 95:1449–1454.
Thivierge, K, Cotton, S, Dufresne, PJ, Mathieu, I, Beauchemin, C, Ide, C, Fortin, MG, Laliberte, JF. Eukaryotic elongation factor 1A interacts with Turnip mosaic virus RNA‐dependent RNA polymerase and VPg‐Pro in virus‐induced vesicles. Virology 2008, 377:216–225.
Olarewaju, O, Ortiz, PA, Chowdhury, WQ, Chatterjee, I, Kinzy, TG. The translation elongation factor eEF1B plays a role in the oxidative stress response pathway. RNA Biol 2004, 1:89–94.
Koonin, EV, Mushegian, AR, Tatusov, RL, Altschul, SF, Bryant, SH, Bork, P, Valencia, A. Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain–study of a diverse, ancient protein superfamily using motif search and structural modeling. Protein Sci 1994, 3:2045–2054.
Kobayashi, S, Kidou, S, Ejiri, S. Detection and characterization of glutathione S‐transferase activity in rice EF‐1betabeta`gamma and EF‐1gamma expressed in Escherichia coli. Biochem Biophys Res Commun 2001, 288:509–514.
Vickers, TJ, Wyllie, S, Fairlamb, AH. Leishmania major elongation factor 1B complex has trypanothione S‐transferase and peroxidase activity. J Biol Chem 2004, 279:49003–49009.
Esposito, AM, Kinzy, TG. The eukaryotic translation elongation Factor 1Bgamma has a non‐guanine nucleotide exchange factor role in protein metabolism. J Biol Chem 2010, 285:37995–38004.
Corbi, N, Batassa, EM, Pisani, C, Onori, A, Di Certo, MG, Strimpakos, G, Fanciulli, M, Mattei, E, Passananti, C. The eEF1gamma subunit contacts RNA polymerase II and binds vimentin promoter region. PLoS One 2010, 5:e14481.
Jonusiene, V, Sasnauskiene, S, Juodka, B. The cloning and characterization of Tetrahymena pyriformis translation elongation factor 1b alpha and gamma subunits. Cell Mol Biol Lett 2005, 10:689–696.
Kaitsuka, T, Tomizawa, K, Matsushita, M. Transformation of eEF1Bdelta into heat‐shock response transcription factor by alternative splicing. EMBO Rep 2011, 12:673–681.
Wu, H, Shi, Y, Lin, Y, Qian, W, Yu, Y, Huo, K. Eukaryotic translation elongation factor 1 delta inhibits the ubiquitin ligase activity of SIAH‐1. Mol Cell Biochem 2011, 357:209–215.

Access to this WIREs title is by subscription only.

Recommend to Your
Librarian Now!

The many roles of the eukaryotic elongation factor 1 complex

Browse by Topic

Access to this WIREs title is by subscription only.

The latest WIREs articles in your inbox