InsP(6) binding to PIKK kinases revealed by the cryo-EM structure of an 
SMG1-SMG8-SMG9 complex

Gat, Yair; Schuller, Jan Michael; Lingaraju, Mahesh; Weyher, Elisabeth; Bonneau, Fabien; Strauss, Mike; Murray, Peter J.; Conti, Elena

doi:10.1038/s41594-019-0342-7

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InsP(6) binding to PIKK kinases revealed by the cryo-EM structure of an SMG1-SMG8-SMG9 complex

MPG-Autoren

/persons/resource/persons245076

Gat, Yair
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons98592

Schuller, Jan Michael
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons208952

Lingaraju, Mahesh
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78877

Weyher, Elisabeth
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77784

Bonneau, Fabien
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons137910

Strauss, Mike
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons215416

Murray, Peter J.
Murray, Peter / Immunoregulation, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77867

Conti, Elena
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Gat, Y., Schuller, J. M., Lingaraju, M., Weyher, E., Bonneau, F., Strauss, M., et al. (2019). InsP(6) binding to PIKK kinases revealed by the cryo-EM structure of an SMG1-SMG8-SMG9 complex. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 26(12), 1089-1093. doi:10.1038/s41594-019-0342-7.

Zitierlink: https://hdl.handle.net/21.11116/0000-0005-A0B4-A

Zusammenfassung

We report the 3.45-angstrom 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 (InsP(6)) in the SMG1 kinase. We show that the InsP(6)-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.