Eukaryotic translation elongation factor 1 alpha 1
| EEF1A1 | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| ||||||||||||||||||||||||||||||||||||||||
| Wikidata | ||||||||||||||||||||||||||||||||||||||||
| ||||||||||||||||||||||||||||||||||||||||
Elongation factor 1-alpha 1 (eEF1a1) is a translation elongation protein, expressed across eukaryotes. In humans, it is encoded by the EEF1A1 gene.[5][6]
This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. This isoform is identified as an autoantigen in 66% of patients with Felty's syndrome. This gene has been found to have multiple copies on many chromosomes, some of which, if not all, represent different pseudogenes.[7]
Structure
Mammalian eEF1A possesses two
heat shock.[11]
Function
The eEF1A1 protein is an isoform of the eEF-1 complex alpha subunit, an elongation factor protein, a GTPase, and an actin bundling protein.[7][8][9][14] As an elongation factor, it is known to mediate the recruitment of aminoacyl-tRNA to the A-site of the 80S ribosome during protein synthesis.[8][14][15][16] As a result, this protein is ubiquitously expressed.[8][10][14]
In addition to its role in
transcription.[17]
Moreover, it participates in several processes required for
phosphatidylinositol 4-kinase, which then regulates phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate levels.[14] This protein can also act as a membrane receptor for the cryptic antiadhesive site of fibronectin, thus inhibiting cell anchorage and promoting apoptosis, or anoikis. Though it has not been observed to localize to the cell membrane, it can be found in the outer cell surface.[16] Its role in apoptosis may also contribute to regulation of cell growth and the immune response.[14]
Additional functions of eEF1A1 include: serving as a coactivator of the
heat shock.[11]
Clinical Significance
Upregulation of eEF1A has been reported in
neoplastic disease, may lead to autoimmunity in breast cancer.[14]
As with breast cancer, upregulation of eEF1A expression is associated with
metastatic progression of prostate cancer.[15]
In the case of acute
signaling pathways.[21]
eEF1A1 is downregulated in
amyotrophic lateral sclerosis (ALS).[11]
Interactions
Eukaryotic translation elongation factor 1 alpha 1 has been shown to
interact
with:
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000156508 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037742 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 8812466.
- S2CID 20719684.
- ^ a b "Entrez Gene: EEF1A1 eukaryotic translation elongation factor 1 alpha 1".
- ^ S2CID 12836593.
- ^ S2CID 13579193.
- ^ PMID 25000480.
- ^ PMID 25233275.
- PMID 24688302.
- PMID 11690632.
- ^ PMID 21704614.
- ^ PMID 22355332.
- ^ PMID 22399298.
- ^ PMID 9891082.
- PMID 18799616.
- ^ PMID 25423367.
- ^ PMID 30224719.
- PMID 22931638.
- PMID 11886851.
Further reading
- Madsen HO, Poulsen K, Dahl O, Clark BF, Hjorth JP (Mar 1990). "Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family". Nucleic Acids Research. 18 (6): 1513–6. PMID 2183196.
- Bec G, Kerjan P, Zha XD, Waller JP (Dec 1989). "Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1". The Journal of Biological Chemistry. 264 (35): 21131–7. PMID 2556394.
- Uetsuki T, Naito A, Nagata S, Kaziro Y (Apr 1989). "Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha". The Journal of Biological Chemistry. 264 (10): 5791–8. PMID 2564392.
- Whiteheart SW, Shenbagamurthi P, Chen L, Cotter RJ, Hart GW (Aug 1989). "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha". The Journal of Biological Chemistry. 264 (24): 14334–41. PMID 2569467.
- Wolfson AD, Orlovsky AF, Gladilin KL (Oct 1988). "Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor". FEBS Letters. 238 (2): 262–4. S2CID 45934458.
- Ann DK, Wu MM, Huang T, Carlson DM, Wu R (Mar 1988). "Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha". The Journal of Biological Chemistry. 263 (8): 3546–9. PMID 3346208.
- Brands JH, Maassen JA, van Hemert FJ, Amons R, Möller W (Feb 1986). "The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites". European Journal of Biochemistry. 155 (1): 167–71. PMID 3512269.
- Opdenakker G, Cabeza-Arvelaiz Y, Fiten P, Dijkmans R, Van Damme J, Volckaert G, Billiau A, Van Elsen A, Van der Schueren B, Van den Berghe H (Apr 1987). "Human elongation factor 1 alpha: a polymorphic and conserved multigene family with multiple chromosomal localizations". Human Genetics. 75 (4): 339–44. S2CID 19189698.
- Rao TR, Slobin LI (Mar 1986). "Structure of the amino-terminal end of mammalian elongation factor Tu". Nucleic Acids Research. 14 (5): 2409. PMID 3960725.
- Carvalho MD, Carvalho JF, Merrick WC (Nov 1984). "Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes". Archives of Biochemistry and Biophysics. 234 (2): 603–11. PMID 6568109.
- Shen R, Su ZZ, Olsson CA, Fisher PB (Jul 1995). "Identification of the human prostatic carcinoma oncogene PTI-1 by rapid expression cloning and differential RNA display". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 6778–82. PMID 7542776.
- Reed VS, Wastney ME, Yang DC (Dec 1994). "Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha". The Journal of Biological Chemistry. 269 (52): 32932–6. PMID 7806521.
- Kielbassa K, Müller HJ, Meyer HE, Marks F, Gschwendt M (Mar 1995). "Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431". The Journal of Biological Chemistry. 270 (11): 6156–62. PMID 7890750.
- Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
- Wu-Baer F, Lane WS, PMID 8626763.
- Sanders J, Brandsma M, Janssen GM, Dijk J, Möller W (May 1996). "Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum". Journal of Cell Science. 109 (5): 1113–7. PMID 8743958.
- Welle S, Thornton C, Bhatt K, Krym M (Sep 1997). "Expression of elongation factor-1 alpha and S1 in young and old human skeletal muscle". The Journals of Gerontology. Series A, Biological Sciences and Medical Sciences. 52 (5): B235-9. PMID 9310071.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
- Sheu GT, Traugh JA (Dec 1997). "Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII". The Journal of Biological Chemistry. 272 (52): 33290–7. PMID 9407120.