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CALM2 — EEF2K

Text-mined interactions from Literome

McLeod et al., FEBS Lett 2001 : eEF2 kinase activity in ARVC extracts was completely dependent upon Ca ( 2+ ) /calmodulin
Dorovkov et al., Biochemistry 2002 : eEF-2K requires calmodulin for activity at neutral as well as acidic pH
Rose et al., J Physiol 2005 : However, skeletal muscle eEF2 kinase was potently activated by Ca(2) ( + ) -calmodulin in vitro, suggesting that the higher eEF2 phosphorylation in working skeletal muscle is mediated by allosteric activation of eEF2 kinase by Ca(2) ( + ) signalling via calmodulin
Ryazanov et al., FEBS Lett 1991 : Among the various modifications of elongation factors, phosphorylation of eEF-2 by the specific Ca2+calmodulin dependent eEF-2 kinase is the best studied and perhaps the most important mechanism of regulation of elongation rate
Ryazanov et al., New Biol 1990 (Adrenal Gland Neoplasms...) : eEF-2 is the target for a very specific Ca2+/calmodulin dependent eEF-2 kinase
Price et al., FEBS Lett 1991 : The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca2+/calmodulin dependent eEF-2 kinase in vitro have been identified
Severinov et al., New Biol 1990 : Phosphorylation of translation elongation factor 2 ( eEF-2 ) by a specific Ca2+/calmodulin dependent eEF-2 kinase plays an important role in the regulation of protein synthesis in mammalian cells
Palmquist et al., FEBS Lett 1994 : Interaction of the calcium and calmodulin regulated eEF-2 kinase with heat shock protein 90
Abdelmajid et al., Int J Dev Biol 1993 : In this paper, we establish the presence of Ca2+/calmodulin dependent kinase III or eEF-2 kinase in these oocytes and describe how the protein synthesis inhibitor emetine is able to release them from the metaphase block
Redpath et al., Biochem J 1993 : The catalytic subunit of cyclic AMP dependent protein kinase (PKA) phosphorylated purified calcium/calmodulin dependent eukaryotic elongation factor-2 (eEF-2) kinase , isolated from rabbit reticulocyte lysates
Redpath et al., J Biol Chem 1996 : A cDNA from rat skeletal muscle encoding calcium/calmodulin dependent eukaryotic elongation factor-2 kinase ( eEF-2K ) has been cloned and sequenced, and the amino acid sequence of the protein has been deduced
Laitusis et al., Arch Biochem Biophys 1998 : L-type Ca2+ channel activity of GH3 pituitary cells, which are enriched in calmodulin dependent eEF-2 kinase , was manipulated such that the impact of [Ca2+ ] i on eEF-2 phosphorylation and translational rate could be examined for up to 10 min without inhibiting initiation