InsP6 binding to PIKK kinases revealed by the cryo-EM structure of an SMG1–SMG8–SMG9 complex
Copyright policy )InsP6 binding to PIKK kinases revealed by the cryo-EM structure of an SMG1–SMG8–SMG9 complex
We report the 3.45-Å resolution cryo-EM structure of human SMG1-SMG8-SMG9, a phosphatidylinositol-3-kinase (PI(3)K)-related protein kinase (PIKK) complex central to messenger RNA surveillance. Structural and MS analyses reveal the presence of inositol hexaphosphate (InsP6) in the SMG1 kinase. We show that the InsP6-binding site is conserved in mammalian target of rapamycin (mTOR) and potentially other PIKK members, and that it is required for optimal in vitro phosphorylation of both SMG1 and mTOR substrates.
- Max Planck Society Germany
- Max Planck Institute of Biochemistry Germany
- McGill University Canada
Models, Molecular, Binding Sites, Phytic Acid, Protein Conformation, RNA Stability, Cryoelectron Microscopy, Intracellular Signaling Peptides and Proteins, Protein Serine-Threonine Kinases, HEK293 Cells, Humans, Protein Multimerization, Protein Kinases, Protein Binding
Models, Molecular, Binding Sites, Phytic Acid, Protein Conformation, RNA Stability, Cryoelectron Microscopy, Intracellular Signaling Peptides and Proteins, Protein Serine-Threonine Kinases, HEK293 Cells, Humans, Protein Multimerization, Protein Kinases, Protein Binding
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