The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein

Kahns, Søren; Lund, Ann; Kristensen, Peter; Knudsen, Charlotte R.; Clark, Brian F. C.; Cavallius, Jens; Merrick, William C.

doi:10.1093/nar/26.8.1884

Cited by 119 publications

(121 citation statements)

References 48 publications

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“…Elongation factor 1-α 2 (EEF1A2) K55 and K165 are known to contain trimethylation by similarity with its ortholog in rabbit, 27 while they were identified as dimethylation sites in our studies. We compared our data to the two other published large-scale lysine acetylation and ubiquitylation data sets.…”

Section: Resultsmentioning

confidence: 58%

Large-scale global identification of protein lysine methylation in vivo

Arnaudo²,

2013

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Section: Resultsmentioning

confidence: 58%

Large-scale global identification of protein lysine methylation in vivo

Arnaudo²,

2013

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“…We also analyzed the effects of exogenous expression of eEF1A2, a homolog of eEF1A1. 29 In C32 cells, expression of endogenous eEF1A2 was undetectable (Supplementary Figure S3), and exogenous expression of eEF1A2, which inhibits the cell death in tetraploids as well as eEF1A1 (data not shown), was shown to similarly increase the number of binucleated cells (Figure 7b). From these data, the cell death machinery is suggested to contribute to eliminate naturally arising binucleated tetraploid cells.…”

Section: Resultsmentioning

confidence: 89%

“…29 eEF1A2 was reported to be exclusively expressed in brain, heart, and skeletal muscle, whereas eEF1A1 is well known to be ubiquitously expressed. 33 We confirmed that the expression of eEF1A2 was undetectable in cell lines used here (Supplementary Figure S3), suggesting that downregulation of eEF1A1 expression in tetraploid cells generally induces loss of eEF1A expression resulting in severe inhibition of translation.…”

Section: Discussionmentioning

confidence: 99%

Novel cell death by downregulation of eEF1A1 expression in tetraploids

Kobayashi

Yonehara

2008

Cell Death Differ

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When duplicated sister chromatids are not properly compacted in mitosis, chromosomes are mis-segregated, inducing genetically unstable tetraploidy known to facilitate aneuploid malignancies. Here, we show that tetraploid cells produced by impaired chromosomal condensation are eliminated by a novel type of cell death different from caspase-dependent apoptosis. The cell death was associated with downregulation of eukaryotic translation elongation factor-1 a 1 (eEF1A1/EF-1a) expression in conjunction with accumulation of its mRNA in processing bodies (P bodies). Importantly, expression of exogenous eEF1A1 was shown to inhibit the caspase-independent cell death, and a similar cell death was observed after inducing the expression of short hairpin RNA specific for eEF1A1. Furthermore, the number of spontaneously arising binucleated cells was indicated to increase several fold during 1-to 2-week cultivation after initiation of exogenous eEF1A expression. Taken together, the novel cell death machinery should help to eliminate abnormal tetraploid cells and inhibit tumorigenesis.

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“…This suggests that other factors, such as the M 4 mAChR, may act to regulate nucleotide exchange of eEF1A2 in compartments lacking eEF1B␣. eEF1A2 functions as an essential factor in protein synthesis as demonstrated by its activity in poly(U)-directed polyphenylalanine synthesis assay (38). Its proposed mechanism of action is as follows.…”

Section: Discussionmentioning

confidence: 99%

Novel Interaction between the M4 Muscarinic Acetylcholine Receptor and Elongation Factor 1A2

McClatchy¹,

Knudsen²,

Clark³

et al. 2002

Journal of Biological Chemistry

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The activation of the muscarinic acetylcholine receptor (mAChR) family, consisting of five subtypes (M 1 -M 5 ), produces a variety of physiological effects throughout the central nervous system. However, the role of each individual subtype remains poorly understood. To further elucidate signal transduction pathways for specific subtypes, we used the most divergent portion of the subtypes, the intracellular third (i3) loop, as bait to identify interacting proteins. Using a brain pull-down assay, we identify elongation factor 1A2 (eEF1A2) as a specific binding partner to the i3 loop of M 4 , and not to M 1 or M 2 .In addition, we demonstrate a direct interaction between these proteins. In the rat striatum, the M 4 mAChR colocalizes with eEF1A2 in the soma and neuropil. In PC12 cells, endogenous eEF1A2 co-immunoprecipitates with the endogenous M 4 mAChR, but not with the endogenous M 1 mAChR. In our in vitro model, M 4 dramatically accelerates nucleotide exchange of eEF1A2, a GTP-binding protein. This indicates the M 4 mAChR is a guanine exchange factor for eEF1A2. eEF1A2 is an essential GTP-binding protein for protein synthesis. Thus, our data suggest a novel role for M 4 in the regulation of protein synthesis through its interaction with eEF1A2.In the central nervous system, the muscarinic acetylcholine receptors (mAChR) 1 play crucial roles in learning, memory, movement, analgesia, and sleep (1-3). Dysfunction in mAChR signaling has been implicated in brain disorders, including Alzheimer's disease, Parkinson's disease, and schizophrenia (4 -6). The mAChRs belong to the G-protein-coupled receptor (GPCR) superfamily. Upon agonist binding, GPCRs bind and activate heterotrimeric G-proteins, which in turn activate various downstream targets. There are two distinct, well characterized G-protein signaling pathways activated by the five mAChR subtypes. M 1 , M 3 , and M 5 couple to G q , which stimulates phospholipase C-␤, and thus releases calcium from intracellular stores and activates protein kinase C (7, 8). M 2 and M 4 are coupled to G i/o , which regulates adenylate cyclase (9). These subtypes are expressed throughout the brain, and, in some brain regions, multiple subtypes are expressed in individual neurons (10). The diversity of physiological effects and the overlapping expression pattern of the muscarinic receptor subtypes suggest that there are signaling pathways initiated by the mAChRs independent of these two heterotrimeric G-protein pathways.Signaling pathways independent of heterotrimeric G-proteins have been reported throughout the GPCR superfamily (11-14). Evidence supporting this hypothesis stems from the identification of novel binding partners of GPCRs other than the traditional heterotrimeric G-proteins. Within the muscarinic family in particular, there is an especially large body of evidence to suggest the existence of nontraditional signaling pathways. There are many reports of G-protein-independent regulation of ion channels by mAChRs (15-18). Moreover, the M 3 mAChR has been found to associate ...

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The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein

Cited by 119 publications

References 48 publications

Large-scale global identification of protein lysine methylation in vivo

Large-scale global identification of protein lysine methylation in vivo

Novel cell death by downregulation of eEF1A1 expression in tetraploids

Novel Interaction between the M4 Muscarinic Acetylcholine Receptor and Elongation Factor 1A2

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