Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase

By Xuemin Wang, Wei Li, Michayla R Williams, N. Terada, D. Alessi, C. Proud. EMBO Journal, 2001

854 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7e23be4d7ccee0a7d50ce676ef287179c35d1f51

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Citations in the corpus

TOR signaling in growth and metabolism. (2006, background): “It also remains to be determined if and how S6K controls translation other than via regulation of elongation factor 2 kinase (eEF2K; Wang et al., 2001).”
The RSK family of kinases: emerging roles in cellular signalling (2008, positive): “Finally, RSK was also shown to phosphorylate the elongation factor-2 (EF2) kinas”
The Molecular Bases of Training Adaptation (2007, background): “Regulation of ribosomal protein synthesis is controlled by phosphorylation events altering mRNA translation initiation, elongation and termination, and the cellular ribosome content which determines the synthesis of protein per mRNA (Farrell et al. 2000; Wang et al. 2001; Hannan et al. 2003; Richter”
Growing roles for the mTOR pathway. (2005, background): “Several S6K1 substrates have been described, including the ribosomal S6 protein, and the translational regulators eEF2 kinase and eIF-4B [32,33].”
mTOR: from growth signal integration to cancer, diabetes and ageing (2010, background): “When phosphorylated by mTORC1, S6K1 promotes mRNA translation by phosphorylating or binding multiple proteins, including eukaryotic elongation factor 2 kinase (eEF2K”
The molecular basis of skeletal muscle atrophy. (2004, background): “Phosphorylation of eEF2 by eEF2K results in a global reduction in ribosomal capacity (100).”
Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. (2002, background): “…of ribosomal protein S6, other targets of S6K1 include the transcription factor CREM- (de Groot et al. 1994), the RNA splicing/export factor CBP80 (Wilson et al. 2000), the translation elongation regulator eEF2 kinase (Wang et al. 2001), and the proapoptotic protein BAD (Harada et al. 2001; Fig.”
The PTEN–PI3K pathway: of feedbacks and cross-talks (2008, background): “mTORC1 phosphorylates and activates S6 kinases 1 and 2 (Guertin and Sabatini, 2007), which in turn activates protein translation and ribosome biogenesis through phosphorylation of different substrates in addition to ribosomal protein S6, including PDCD4, eEF2 kinase and eIF4B (Wang et al., 2001; Rau”
Resistance exercise increases AMPK activity and reduces 4E‐BP1 phosphorylation and protein synthesis in human skeletal muscle (2006, background): “In fact, it has recently been suggested that mTOR may regulate eEF2 kinase (Browne & Proud, 2002) since S6K1 can phosphorylate eEF2 kinase, leading to enhanced elongation (Wang et al. 2001).”
Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress (2010, background): “This kinase normally negatively regulates translation elongation by phosphorylating and suppressing eukaryotic elongation factor 2 (eE-F2), and S6K1 relieves this inhibition by directly phosphorylating eEF-2K (Wang et al., 2001).”