ArticleGenetics2010
Drosophila translational elongation factor-1gamma is modified in response to DOA kinase activity and is essential for cellular viability.
Article in Genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Article
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- Role of BicDR in bristle shaft construction and support of BicD functions.Journal of cell science · 2024Article
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- Non-translational Connections of eEF1B in the Cytoplasm and Nucleus of Cancer Cells.Frontiers in molecular biosciences · 2020Review
- Strain-Specific Contribution of Eukaryotic Elongation Factor 1 Gamma to the Translation of Influenza A Virus Proteins.Frontiers in microbiology · 2018Article
- Article
- Targeted Genetic Screen in Amyotrophic Lateral Sclerosis Reveals Novel Genetic Variants with Synergistic Effect on Clinical Phenotype.Frontiers in molecular neuroscience · 2017Article
- Multifunctional RNA processing protein SRm160 induces apoptosis and regulates eye and genital development in Drosophila.Genetics · 2014Article
- Protein kinase Darkener of apricot and its substrate EF1γ regulate organelle transport along microtubules.Journal of cell science · 2014Article
- Transcriptome profiling of sexual maturation and mating in the Mediterranean fruit fly, Ceratitis capitata.PloS one · 2012Article
- Article
- Differential protein modulation in midguts of Aedes aegypti infected with chikungunya and dengue 2 viruses.PloS one · 2010Article
- The role of the Drosophila LAMMER protein kinase DOA in somatic sex determination.Journal of genetics · 2010Article
- The many roles of the eukaryotic elongation factor 1 complex.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Drosophila translational elongation factor-1gamma (EF1gamma) interacts in the yeast two-hybrid system with DOA, the LAMMER protein kinase of Drosophila. Analysis of mutant EF1gamma alleles reveals that the locus encodes a structurally conserved protein essential for both organismal and cellular survival. Although no genetic interactions were detected in combinations with mutations in EF1alpha, an EF1gamma allele enhanced mutant phenotypes of Doa alleles. A predicted LAMMER kinase phosphorylation site conserved near the C terminus of all EF1gamma orthologs is a phosphorylation site in vitro for both Drosophila DOA and tobacco PK12 LAMMER kinases. EF1gamma protein derived from Doa mutant flies migrates with altered mobility on SDS gels, consistent with it being an in vivo substrate of DOA kinase. However, the aberrant mobility appears to be due to a secondary protein modification, since the mobility of EF1gamma protein obtained from wild-type Drosophila is unaltered following treatment with several nonspecific phosphatases. Expression of a construct expressing a serine-to-alanine substitution in the LAMMER kinase phosphorylation site into the fly germline rescued null EF1gamma alleles but at reduced efficiency compared to a wild-type construct. Our data suggest that EF1gamma functions in vital cellular processes in addition to translational elongation and is a LAMMER kinase substrate in vivo.
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