ArticleMolecular and cellular biochemistry2011
Phosphorylation of maize eukaryotic translation initiation factor on Ser2 by catalytic subunit CK2.
Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- Hypusination, a Metabolic Posttranslational Modification of eIF5A in Plants during Development and Environmental Stress Responses.Plants (Basel, Switzerland) · 2021Review
- Article
- iPTMnet: an integrated resource for protein post-translational modification network discovery.Nucleic acids research · 2018Article
- Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation.Scientific reports · 2016Article
- Holophytochrome-Interacting Proteins in Physcomitrella: Putative Actors in Phytochrome Cytoplasmic Signaling.Frontiers in plant science · 2016Article
- Identification of the phosphorylated residues in TveIF5A by mass spectrometry.Genomics, proteomics & bioinformatics · 2013Article
- Photosynthetic control of Arabidopsis leaf cytoplasmic translation initiation by protein phosphorylation.PloS one · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Alignment of eukaryotic translation initiation factor 5A (eIF5A) sequences has shown, for plants, in contrast to most other eukaryotes, the presence of N-terminal serine residue (Ser2) which could be phosphorylated by CK2. Using point directed mutagenesis, we demonstrate here that in recombinant maize ZmeIF5Awt Ser2 is exclusively phosphorylated by catalytic subunit of CK2 (CK2α), whereas its mutated variant Ser2Ala is not phosphorylated. To shed light on the physiological significance of this Ser2 phosphorylation, transient expression of fluorescence-labeled proteins was performed in maize protoplast. Wild-type ZmeIF5A was distributed evenly between nucleus and cytoplasm, but the replacement of Ser2 by aspartic acid, which mimics the phosphorylated serine, influences its intracellular localization. We postulate that phosphorylation of Ser2 in maize eIF5A, and most probably in other plant cells, plays a role in specific regulation of nuclear export of eIF5A-bound mRNAs.
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