| Roles of HDAC2, eIF5, and eIF6 in Lung Cancer Tumorigenesis. | Roles of HDAC2, eIF5, and eIF6 in Lung Cancer Tumorigenesis.
Cai SX, Chen WS, Zeng W, Cheng XF, Lin MB, Wang JS. | 01/8/2022 |
| Translational initiation pathway inhibition could be of clinical utility in male breast cancer patients overexpressing eIF4E and eIF5. With mTOR inhibitors that target this pathway now in the clinic, these biomarkers may represent new targets for therapeutic intervention, although further independent validation is required | A Case-Matched Gender Comparison Transcriptomic Screen Identifies eIF4E and eIF5 as Potential Prognostic Markers in Male Breast Cancer.
Humphries MP, Sundara Rajan S, Droop A, Suleman CAB, Carbone C, Nilsson C, Honarpisheh H, Cserni G, Dent J, Fulford L, Jordan LB, Jones JL, Kanthan R, Litwiniuk M, Di Benedetto A, Mottolese M, Provenzano E, Shousha S, Stephens M, Walker RA, Kulka J, Ellis IO, Jeffery M, Thygesen HH, Cappelletti V, Daidone MG, Hedenfalk IA, Fjällskog ML, Melisi D, Stead LF, Shaaban AM, Speirs V. | 02/24/2018 |
| Data show that eIF5-mimic protein (5MP) represses non-AUG translation by competing with translation initiation factor 5 (eIF5) for the Met-tRNAi-binding factor eIF2. | Competition between translation initiation factor eIF5 and its mimic protein 5MP determines non-AUG initiation rate genome-wide.
Tang L, Morris J, Wan J, Moore C, Fujita Y, Gillaspie S, Aube E, Nanda J, Marques M, Jangal M, Anderson A, Cox C, Hiraishi H, Dong L, Saito H, Singh CR, Witcher M, Topisirovic I, Qian SB, Asano K., Free PMC Article | 12/16/2017 |
| The down-regulation of the GCN4 expression (Gcn(-) phenotype) in the eIF5(G31R) mutant was not because of leaky scanning defects; rather was due to the utilization of upUUG initiation codons at the 5' regulatory region present between uORF1 and the main GCN4 ORF. | Defect in the GTPase activating protein (GAP) function of eIF5 causes repression of GCN4 translation.
Antony A C, Alone PV. | 06/24/2017 |
| overexpression of eIF5 and 5MP induces translation of ATF4 | Overexpression of eIF5 or its protein mimic 5MP perturbs eIF2 function and induces ATF4 translation through delayed re-initiation.
Kozel C, Thompson B, Hustak S, Moore C, Nakashima A, Singh CR, Reid M, Cox C, Papadopoulos E, Luna RE, Anderson A, Tagami H, Hiraishi H, Slone EA, Yoshino KI, Asano M, Gillaspie S, Nietfeld J, Perchellet JP, Rothenburg S, Masai H, Wagner G, Beeser A, Kikkawa U, Fleming SD, Asano K., Free PMC Article | 06/10/2017 |
| it is eIF5-induced GTP hydrolysis and Pi release that irreversibly trap the 48S complex, and this complex is further stabilized by eIF5B and 60S joining. | Sliding of a 43S ribosomal complex from the recognized AUG codon triggered by a delay in eIF2-bound GTP hydrolysis.
Terenin IM, Akulich KA, Andreev DE, Polyanskaya SA, Shatsky IN, Dmitriev SE., Free PMC Article | 07/30/2016 |
| The N-terminal tail of eIF1A mediates the interaction with eIF5 and eIF1. | The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation complexes.
Luna RE, Arthanari H, Hiraishi H, Akabayov B, Tang L, Cox C, Markus MA, Luna LE, Ikeda Y, Watanabe R, Bedoya E, Yu C, Alikhan S, Wagner G, Asano K., Free PMC Article | 03/8/2014 |
| Coordinated movements of eukaryotic translation initiation factors eIF1, eIF1A, and eIF5 trigger phosphate release from eIF2 in response to start codon recognition by the ribosomal preinitiation complex | Coordinated movements of eukaryotic translation initiation factors eIF1, eIF1A, and eIF5 trigger phosphate release from eIF2 in response to start codon recognition by the ribosomal preinitiation complex.
Nanda JS, Saini AK, Muñoz AM, Hinnebusch AG, Lorsch JR., Free PMC Article | 04/27/2013 |
| This study provides mechanistic insight into the role of eIF5-carboxyl terminal domain's dynamic interplay with eIF1 and eIF2beta. | The C-terminal domain of eukaryotic initiation factor 5 promotes start codon recognition by its dynamic interplay with eIF1 and eIF2β.
Luna RE, Arthanari H, Hiraishi H, Nanda J, Martin-Marcos P, Markus MA, Akabayov B, Milbradt AG, Luna LE, Seo HC, Hyberts SG, Fahmy A, Reibarkh M, Miles D, Hagner PR, O'Day EM, Yi T, Marintchev A, Hinnebusch AG, Lorsch JR, Asano K, Wagner G., Free PMC Article | 03/2/2013 |
| miR-5787 represses cell growth, in part, by targeting eIF5. | The hsa-miR-5787 represses cellular growth by targeting eukaryotic translation initiation factor 5 (eIF5) in fibroblasts.
Yoo H, Yoo JK, Lee J, Lee DR, Ko JJ, Oh SH, Choo YK, Kim JK. | 01/28/2012 |
| 3-dimensional solution structure of N-terminal domain of human eIF5, has 2 subdomains, both reminiscent of nucleic-acid-binding modules. N-terminal subdomain contains "arginine finger" motif essential for GAP function. | Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors.
Conte MR, Kelly G, Babon J, Sanfelice D, Youell J, Smerdon SJ, Proud CG. | 01/21/2010 |
| CK2 may be involved in the regulation of cell cycle progression by associating with and phosphorylating a key molecule for translation initiation. | CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cycle progression.
Homma MK, Wada I, Suzuki T, Yamaki J, Krebs EG, Homma Y., Free PMC Article | 01/21/2010 |
| The carboxy-terminal domain (CTD)of eIF5 is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. | The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5.
Bieniossek C, Schütz P, Bumann M, Limacher A, Uson I, Baumann U. | 01/21/2010 |