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

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.

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 Creators:
Gat, Yair1, Author           
Schuller, Jan Michael1, Author           
Lingaraju, Mahesh1, Author           
Weyher, Elisabeth2, Author           
Bonneau, Fabien1, Author           
Strauss, Mike2, Author           
Murray, Peter J.3, Author           
Conti, Elena1, Author           
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              
3Murray, Peter / Immunoregulation, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466696              

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Free keywords: RNA SURVEILLANCE COMPLEX; PIGGYBAC TRANSPOSASE; HUMAN SMG-1; UPF1; ACTIVATION; DOMAIN; PHOSPHORYLATION; ARCHITECTURE; VALIDATION; DECAY
 Abstract: 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.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Issued
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000501349100005
DOI: 10.1038/s41594-019-0342-7
 Degree: -

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Title: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 26 (12) Sequence Number: - Start / End Page: 1089 - 1093 Identifier: ISSN: 1545-9993