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• W2048083639 abstract "Elongation factor 2 (eEF2) is the main regulator of peptide chain elongation in eukaryotic cells. Using sea urchin eggs and early embryos, two isoforms of eEF2 of respectively 80 and 83 kDa apparent molecular weight have been discovered. Both isoforms were identified by immunological analysis as well as mass spectrometry, and appeared to originate from a unique post-translationally modified protein. Accompanying the net increase in protein synthesis that occurs in early development, both eEF2 isoforms underwent dephosphorylation in the 15 min period following fertilization, in accordance with the active role of dephosphorylated eEF2 in regulation of protein synthesis. After initial dephosphorylation, the major 83 kDa isoform remained dephosphorylated while the 80 kDa isoform was progressively re-phosphorylated in a cell-cycle dependent fashion. In vivo inhibition of phosphorylation of the 80 kDa isoform impaired the completion of the first cell cycle of early development implicating the involvement of eEF2 phosphorylation in the exit from mitosis." @default.
• W2048083639 created "2016-06-24" @default.
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• W2048083639 creator A5051231551 @default.
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• W2048083639 date "2011-02-01" @default.
• W2048083639 modified "2023-09-25" @default.
• W2048083639 title "Identification of a new isoform of eEF2 whose phosphorylation is required for completion of cell division in sea urchin embryos" @default.
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• W2048083639 doi "https://doi.org/10.1016/j.ydbio.2010.12.015" @default.
• W2048083639 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21167828" @default.
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