Eukaryotic elongation factor 2 kinase regulates foam cell formation via translation of CD36

2022 ◽  
Vol 36 (2) ◽  
Author(s):  
Sanuja Fernando ◽  
Thalia Salagaras ◽  
Nisha Schwarz ◽  
Lauren Sandeman ◽  
Joanne T. M. Tan ◽  
...  
Keyword(s):  
Foam Cell ◽  
Cell Formation ◽  
Elongation Factor ◽  
Foam Cell Formation ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

scholarly journals Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

2019 ◽  
Vol 74 (1) ◽  
pp. 88-100.e9 ◽  
Author(s):  
Leonie Mönkemeyer ◽  
Courtney L. Klaips ◽  
David Balchin ◽  
Roman Körner ◽  
F. Ulrich Hartl ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Chaperone Function ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

Eukaryotic Elongation Factor 2 (eEF2) is a Potential Biomarker of Prostate Cancer

2017 ◽  
Vol 24 (4) ◽  
pp. 885-890 ◽  
Author(s):  
Xuefeng Zhang ◽  
Linkun Hu ◽  
Mingzhan Du ◽  
Xuedong Wei ◽  
Jun Zhang ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Elongation Factor ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor ◽  
Potential Biomarker

scholarly journals Insights into the regulation of eukaryotic elongation factor 2 kinase and the interplay between its domains

2012 ◽  
Vol 442 (1) ◽  
pp. 105-118 ◽  
Author(s):  
Craig R. Pigott ◽  
Halina Mikolajek ◽  
Claire E. Moore ◽  
Stephen J. Finn ◽  
Curtis W. Phippen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Catalytic Domain ◽  
Functional Organization ◽  
Elongation Factor ◽  
Kinase Domain ◽  
Conserved Residues ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Kinase Catalytic Domain ◽  
Eukaryotic Elongation Factor

eEF2K (eukaryotic elongation factor 2 kinase) is a Ca2+/CaM (calmodulin)-dependent protein kinase which regulates the translation elongation machinery. eEF2K belongs to the small group of so-called ‘α-kinases’ which are distinct from the main eukaryotic protein kinase superfamily. In addition to the α-kinase catalytic domain, other domains have been identified in eEF2K: a CaM-binding region, N-terminal to the kinase domain; a C-terminal region containing several predicted α-helices (resembling SEL1 domains); and a probably rather unstructured ‘linker’ region connecting them. In the present paper, we demonstrate: (i) that several highly conserved residues, implicated in binding ATP or metal ions, are critical for eEF2K activity; (ii) that Ca2+/CaM enhance the ability of eEF2K to bind to ATP, providing the first insight into the allosteric control of eEF2K; (iii) that the CaM-binding/α-kinase domain of eEF2K itself possesses autokinase activity, but is unable to phosphorylate substrates in trans; (iv) that phosphorylation of these substrates requires the SEL1-like domains of eEF2K; and (v) that highly conserved residues in the C-terminal tip of eEF2K are essential for the phosphorylation of eEF2, but not a peptide substrate. On the basis of these findings, we propose a model for the functional organization and control of eEF2K.

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