Specific interaction between S6K1 and CoA synthase: a potential link between the mTOR/S6K pathway, CoA biosynthesis and energy metabolism.
Ribosomal protein S6 kinase (S6K) is a key regulator of cell size and growth. It is regulated via phosphoinositide 3-kinases (PI3K) and the mammalian target of rapamycin (mTOR) signaling pathways. We demonstrate for the first time that CoA synthase associates specifically with S6K1. The association was observed between native and ... transiently overexpressed proteins in vivo, as well as by BIAcore analysis in vitro. The sites of interaction were mapped to the C-terminal regions of both CoA synthase and S6K1. In vitro studies indicated that the interaction does not affect their enzymatic activities and that CoA synthase is not a substrate for S6 kinase. This study uncovers a potential link between mTor/S6K signaling pathway and energy metabolism through CoA and its thioester derivatives, but its physiological relevance should be further elucidated.
Mesh Terms:
1-Phosphatidylinositol 3-Kinase, Acetate-CoA Ligase, Amino Acid Sequence, Breast Neoplasms, Cell Line, Cell Line, Tumor, Cell Size, Energy Metabolism, Female, Humans, Protein Kinases, Ribosomal Protein S6 Kinases, Signal Transduction, Surface Plasmon Resonance
1-Phosphatidylinositol 3-Kinase, Acetate-CoA Ligase, Amino Acid Sequence, Breast Neoplasms, Cell Line, Cell Line, Tumor, Cell Size, Energy Metabolism, Female, Humans, Protein Kinases, Ribosomal Protein S6 Kinases, Signal Transduction, Surface Plasmon Resonance
FEBS Lett.
Date: Dec. 17, 2004
PubMed ID: 15589845
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