Effect of point mutations of regulatory aminoacids residues and N- and C-terminal deletions of S6K1 and S6K2 on kinase activity

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 mutagenesi...

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Bibliographic Details
Published in:Biopolimery i kletka 2005-01, Vol.21 (1), p.42-47
Main Authors: Valovka, T. I., Gout, I. T., Filonenko, V. V.
Format: Article
Language:English
Subjects:
Homology
Kinases
Phosphorylation
Ribosomal protein S6
Site-directed mutagenesis
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Summary: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.
ISSN:0233-7657
1993-6842
DOI:10.7124/bc.0006DA