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Article

Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.

The EMBO journal - 3 Apr 2018

Brandmann Tobias, Fakim Hana, Padamsi Zoya, Youn Ji-Young, Gingras Anne-Claude, Fabian Marc R, Jinek Martin

Abstract excerpt

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...

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Share to Caenorhabditis elegans
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 29510985
DOI: 10.15252/embj.201797869
PMCID: PMC5881628

Genes

DDX6

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

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