| eEF1A2 promotes PTEN-GSK3beta-SCF complex-dependent degradation of Aurora kinase A and is inactivated in breast cancer. | eEF1A2 promotes PTEN-GSK3β-SCF complex-dependent degradation of Aurora kinase A and is inactivated in breast cancer.
Treekitkarnmongkol W, Solis LM, Sankaran D, Gagea M, Singh PK, Mistry R, Nguyen T, Kai K, Liu J, Sasai K, Jitsumori Y, Liu J, Nagao N, Stossi F, Mancini MA, Wistuba II, Thompson AM, Lee JM, Cadiñanos J, Wong KK, Abbott CM, Sahin AA, Liu S, Katayama H, Sen S. | 03/14/2024 |
| Face-valid phenotypes in a mouse model of the most common mutation in EEF1A2-related neurodevelopmental disorder. | Face-valid phenotypes in a mouse model of the most common mutation in EEF1A2-related neurodevelopmental disorder.
Marshall GF, Fasol M, Davies FCJ, Le Seelleur M, Fernandez Alvarez A, Bennett-Ness C, Gonzalez-Sulser A, Abbott CM., Free PMC Article | 02/12/2024 |
| Autism- and epilepsy-associated EEF1A2 mutations lead to translational dysfunction and altered actin bundling. | Autism- and epilepsy-associated EEF1A2 mutations lead to translational dysfunction and altered actin bundling.
Mohamed MS, Klann E., Free PMC Article | 09/28/2023 |
| Endogenous epitope tagging of eEF1A2 in mice reveals early embryonic expression of eEF1A2 and subcellular compartmentalisation of neuronal eEF1A1 and eEF1A2. | Endogenous epitope tagging of eEF1A2 in mice reveals early embryonic expression of eEF1A2 and subcellular compartmentalisation of neuronal eEF1A1 and eEF1A2.
Davies FCJ, Marshall GF, Pegram E, Gadd D, Abbott CM. | 09/7/2023 |
| Loss of eEF1A2 (Eukaryotic Elongation Factor 1 A2) in Murine Myocardium Results in Dilated Cardiomyopathy. | Loss of eEF1A2 (Eukaryotic Elongation Factor 1 A2) in Murine Myocardium Results in Dilated Cardiomyopathy.
Feng W, Wang L, Veevers J, Liu C, Huang T, Chen J., Free PMC Article | 12/25/2021 |
| Recapitulation of the EEF1A2 D252H neurodevelopmental disorder-causing missense mutation in mice reveals a toxic gain of function. | Recapitulation of the EEF1A2 D252H neurodevelopmental disorder-causing missense mutation in mice reveals a toxic gain of function.
Davies FCJ, Hope JE, McLachlan F, Marshall GF, Kaminioti-Dumont L, Qarkaxhija V, Nunez F, Dando O, Smith C, Wood E, MacDonald J, Hardt O, Abbott CM. | 08/14/2021 |
| The presence of G70S protein was not sufficient to protect mice from neurodegeneration in G70S/- eEF1A2 mice, showing that the mutant protein is essentially non-functional. | Biallelic mutations in the gene encoding eEF1A2 cause seizures and sudden death in F0 mice.
Davies FC, Hope JE, McLachlan F, Nunez F, Doig J, Bengani H, Smith C, Abbott CM., Free PMC Article | 12/1/2018 |
| This provides the first in vivo confirmation that eEF1A2 plays an important role in translation. | In vivo characterization of the role of tissue-specific translation elongation factor 1A2 in protein synthesis reveals insights into muscle atrophy.
Doig J, Griffiths LA, Peberdy D, Dharmasaroja P, Vera M, Davies FJ, Newbery HJ, Brownstein D, Abbott CM., Free PMC Article | 03/29/2014 |
| Heterozygous mutant mice showed no deficit in neuromuscular function or signs of spinal cord pathology, in spite of the low levels of eEF1A2 | Haploinsufficiency for translation elongation factor eEF1A2 in aged mouse muscle and neurons is compatible with normal function.
Griffiths LA, Doig J, Churchhouse AM, Davies FC, Squires CE, Newbery HJ, Abbott CM., Free PMC Article | 01/12/2013 |
| In-depth analysis using site-directed mutagenesis revealed that PKCbetaI could phosphorylate Ser(3) of the eEF1A2 isoform and that the association between eEF1A2 and PKCbetaI was dependent on the phosphorylation status of eEF1A2 | eEF1A phosphorylation in the nucleus of insulin-stimulated C2C12 myoblasts: Ser⁵³ is a novel substrate for protein kinase C βI.
Piazzi M, Bavelloni A, Faenza I, Blalock W, Urbani A, D'Aguanno S, Fiume R, Ramazzotti G, Maraldi NM, Cocco L., Free PMC Article | 04/9/2011 |
| EEF1A2 may play contribute to the induction or progression of some plasmacytomas and a small percentage of multiple myeloma. | Eef1a2 promotes cell growth, inhibits apoptosis and activates JAK/STAT and AKT signaling in mouse plasmacytomas.
Li Z, Qi CF, Shin DM, Zingone A, Newbery HJ, Kovalchuk AL, Abbott CM, Morse HC 3rd., Free PMC Article | 09/13/2010 |
| these results suggest an important role for eEF1A2 in driving cap-independent translation of utrophin A in skeletal muscle. | The utrophin A 5'-UTR drives cap-independent translation exclusively in skeletal muscles of transgenic mice and interacts with eEF1A2.
Miura P, Coriati A, Bélanger G, De Repentigny Y, Lee J, Kothary R, Holcik M, Jasmin BJ. | 05/31/2010 |
| The above findings suggest that an increase in free-form eEF1A under alkaline conditions plays a critical role in alkalinization-induced cell growth. | The role of translation elongation factor eEF1A in intracellular alkalinization-induced tumor cell growth.
Kim J, Namkung W, Yoon JS, Jo MJ, Lee SH, Kim KH, Kim JY, Lee MG. | 01/21/2010 |
| eEF1A-2 interacts with Prdx-I to functionally provide cells with extraordinary resistance to oxidative stress-induced cell death[eEF1A-2 and Prdx-I] | Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress.
Chang R, Wang E. | 01/21/2010 |
| This is a putative oncogene in ovarian cancer. | Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer.
Anand N, Murthy S, Amann G, Wernick M, Porter LA, Cukier IH, Collins C, Gray JW, Diebold J, Demetrick DJ, Lee JM. | 01/21/2010 |
| expression of eEF1A-2/S1 protein is activated upon myogenic differentiation | Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis.
Ruest LB, Marcotte R, Wang E., Free PMC Article | 01/21/2010 |
| Data suggest that spontaneous failure of eEF1A2 expression in the wasted mutant first triggers gliosis in spinal cord and retraction of motor nerve terminals in muscle, and then motor neuron pathology and death. | Progressive loss of motor neuron function in wasted mice: effects of a spontaneous null mutation in the gene for the eEF1 A2 translation factor.
Newbery HJ, Gillingwater TH, Dharmasaroja P, Peters J, Wharton SB, Thomson D, Ribchester RR, Abbott CM. | 01/21/2010 |