期刊
EMBO JOURNAL
卷 37, 期 7, 页码 -出版社
WILEY
DOI: 10.15252/embj.201797869
关键词
mRNA decapping; P-bodies; protein-protein interaction networks; SLIMs; translational repression
资金
- European Research Council (ERC) Starting Grant ANTIVIRNA [ERC-StG-337284]
- Canadian Institutes of Health Research (CIHR) [MOP-130425]
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN-2015-03712]
- NSERC Discovery and Accelerator Supplement [RGPIN-2014-06434, RGPAS 462169]
- Fonds de recherche du QuebecSante (FRQS) Chercheur-Boursier Junior 1
- CIHR New Investigator awards
The LSM domain-containing protein LSM14/Rap55 plays a role in mRNA decapping, translational repression, and RNA granule (P-body) assembly. How LSM14 interacts with the mRNA silencing machinery, including the eIF4E-binding protein 4E-T and the DEAD-box helicase DDX6, is poorly understood. Here we report the crystal structure of the LSM domain of LSM14 bound to a highly conserved C-terminal fragment of 4E-T. The 4E-T C-terminus forms a bi-partite motif that wraps around the N-terminal LSM domain of LSM14. We also determined the crystal structure of LSM14 bound to the C-terminal RecA-like domain of DDX6. LSM14 binds DDX6 via a unique non-contiguous motif with distinct directionality as compared to other DDX6-interacting proteins. Together with mutational and proteomic studies, the LSM14-DDX6 structure reveals that LSM14 has adopted a divergent mode of binding DDX6 in order to support the formation of mRNA silencing complexes and P-body assembly.
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