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• W2030589634 startingPage "658" @default.
• W2030589634 abstract "A variety of cellular processes rely on G-proteins, which cycle through active GTP-bound and inactive GDP-bound forms. The switch between these states is commonly regulated by GEFs (guanine-nucleotide-exchange factors) and GAPs (GTPase-activating proteins). Although G-proteins have structural similarity, GEFs are very diverse proteins. A complex example of this system is seen in eukaryotic translation initiation between eIF (eukaryotic initiation factor) 2, a G-protein, its five-subunit GEF, eIF2B, and its GAP, eIF5. eIF2 delivers Met-tRNAi (initiator methionyl-tRNA) to the 40S ribosomal subunit before mRNA binding. Upon AUG recognition, eIF2 hydrolyses GTP, aided by eIF5. eIF2B then re-activates eIF2 by removing GDP, thereby promoting association of GTP. In the present article, we review data from studies of representative G-protein–GEF pairs and compare these with observations from our research on eIF2 and eIF2B to propose a model for how interactions between eIF2B and eIF2 promote guanine nucleotide exchange." @default.
• W2030589634 created "2016-06-24" @default.
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• W2030589634 creator A5064877363 @default.
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• W2030589634 date "2008-07-22" @default.
• W2030589634 modified "2023-10-15" @default.
• W2030589634 title "Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiation" @default.
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• W2030589634 doi "https://doi.org/10.1042/bst0360658" @default.
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