Biopolym. Cell. 2005; 21(1):42-47.
Cell Biology
Effect of point mutations of regulatory aminoacids residues and N- and C-terminal deletions of S6K1 and S6K2 on kinase activity
- Ludwig Institute for Cancer Research
91 Riding house str., London, UK, WIP8BT - Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
Abstract
The family of ribosomal protein S6 kinases includes two forms –
S6K1 and S6K2 that share high level of structural homology towards
catalytic domains. Existence of homological phosphorylation sites
suggests the functioning of similar mechanisms of the kinase
activation. Using site-directed mutagenesis and N-, C-terminal
deleting of S6K it has been demonstrated that phosphorylation of
Thr412 and Thr401 are necessary for the full activation of S61 and
S62 correspondent. Different sensitivity of S6K to the inhibitory
actions of rapamicine relates to the structure of C- terminal S6K
regions that exhibits low homology.
Keywords: ribosomal protein 56, S6K1 and S6K2, site-directed mutagenesis
Full text: (PDF, in Ukrainian)
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