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- W175655779 abstract "Eukaryotic Elongation Factor 1A (eEF1A) is an abundant G-protein whose primary function is to transport aminoacyl-tRNA to elongating ribosomes during eukaryotic translation. Additionally, eEF1A has also been identified as an actin-binding protein. This second property of eEF1A allows it to bind and subsequently bundle filamentous actin into two specific structures: patches and cables. These structures collectively referred to as the actin cytoskeleton, provide the network for intracellular transport and endocytosis in yeast. Evidence has substantiated the eEF1A-actin interaction; however, regulation of this association has yet to be determined. Two major regulators of translation in yeast are the TOR kinases and Gcn2p. These kinases are activated in response to nutrient and amino acid starvation, respectively, and ultimately lead to decreased translation via blocked initiation. Using strains expressing either an F308L or S405P mutant form of eEF1A, both of which exhibit disorganized actin cytoskeletons and blocked translation initiation, we analyzed the affects of TOR and Gcn2p on the eEF1A-actin interaction. Our current findings suggest that while eEF1A and TOR appear to promote actin cytoskeleton integrity through two distinct pathways, Gcn2p may be involved in eEF1A's ability to sustain actin organization. This research was supported by the National Institutes of Health." @default.
- W175655779 created "2016-06-24" @default.
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- W175655779 date "2010-04-01" @default.
- W175655779 modified "2023-09-26" @default.
- W175655779 title "Translation Regulators Mediate the Interaction between Eukaryotic Elongation Factor 1A and the Actin Cytoskeleton in Saccharomyces cerevisiae" @default.
- W175655779 doi "https://doi.org/10.1096/fasebj.24.1_supplement.467.3" @default.
- W175655779 hasPublicationYear "2010" @default.
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